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<dc:rights>© 2009 Nature Publishing Group</dc:rights>
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<title>The EMBO Journal</title>
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<title>Oncogene and tumour suppressor: the two faces of SnoN</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/3MXzYuXkLJE/emboj.2009.311</link>
<description>EMBO J2822, 3500–3513 (2009); published online 10 September 2009SnoN was first identified based on its homology with the proto-oncogene c-Ski, and has since been implicated as a promoter of oncogenic transformation and cancer progression. Consistent with a role as proto-oncogene, SnoN negatively regulates TGF-β signalling, through its interactions with Smad complexes. Thus, SnoN inhibits the growth inhibitory effect of TGF-β, which is considered as the basis for the tumour suppressor activity of TGF-β signalling. In this issue of The EMBO Journal, Pan et al (2009) now demonstrate that SnoN also functions as a tumour suppressor, independently of its role in Smad signalling. The tumour suppressor role of SnoN results from its interaction with the promyelocytic leukaemia (PML) protein and the accumulation of SnoN in PML nuclear bodies, thus allowing SnoN to stabilize p53 and induce premature senescence.</description>
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<p>
<b>Oncogene and tumour suppressor: the two faces of SnoN</b>
</p>
<p>The EMBO Journal 28, 3459 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.311">doi:10.1038/emboj.2009.311</a>
</p>
<p>Authors: Samy Lamouille &amp; Rik Derynck</p>
<p>EMBO J2822, 3500&#8211;3513 (2009); published online 10 September 2009SnoN was first identified based on its homology with the proto-oncogene c-Ski, and has since been implicated as a promoter of oncogenic transformation and cancer progression. Consistent with a role as proto-oncogene, SnoN negatively regulates TGF-&#946; signalling, through its interactions with Smad complexes. Thus, SnoN inhibits the growth inhibitory effect of TGF-&#946;, which is considered as the basis for the tumour suppressor activity of TGF-&#946; signalling. In this issue of The EMBO Journal, Pan et al (2009) now demonstrate that SnoN also functions as a tumour suppressor, independently of its role in Smad signalling. The tumour suppressor role of SnoN results from its interaction with the promyelocytic leukaemia (PML) protein and the accumulation of SnoN in PML nuclear bodies, thus allowing SnoN to stabilize p53 and induce premature senescence.</p>
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<dc:title>Oncogene and tumour suppressor: the two faces of SnoN</dc:title>
<dc:creator>Samy Lamouille</dc:creator>
<dc:creator>Rik Derynck</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.311</dc:identifier>
<dc:source>The EMBO Journal 28, 3459 (2009)</dc:source>
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<prism:section>Have you seen ...?</prism:section>
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<item rdf:about="http://dx.doi.org/10.1038/emboj.2009.280">
<title>A ribosome–nascent chain sensor of membrane protein biogenesis in Bacillus subtilis</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/eQm_qEMkGBQ/emboj.2009.280</link>
<description>Proteins in the YidC/Oxa1/Alb3 family have essential functions in membrane protein insertion and folding. Bacillus subtilis encodes two YidC homologs, one that is constitutively expressed (spoIIIJ/yidC1) and a second (yqjG/yidC2) that is induced in spoIIIJ mutants. Regulated induction of </description>
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<p>
<b>A ribosome&#8211;nascent chain sensor of membrane protein biogenesis in Bacillus subtilis</b>
</p>
<p>The EMBO Journal 28, 3461 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.280">doi:10.1038/emboj.2009.280</a>
</p>
<p>Authors: Shinobu Chiba, Anne Lamsa &amp; Kit Pogliano</p>
<p>Proteins in the YidC/Oxa1/Alb3 family have essential functions in membrane protein insertion and folding. Bacillus subtilis encodes two YidC homologs, one that is constitutively expressed (spoIIIJ/yidC1) and a second (yqjG/yidC2) that is induced in spoIIIJ mutants. Regulated induction of </p>
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<dc:title>A ribosome–nascent chain sensor of membrane protein biogenesis in Bacillus subtilis</dc:title>
<dc:creator>Shinobu Chiba</dc:creator>
<dc:creator>Anne Lamsa</dc:creator>
<dc:creator>Kit Pogliano</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.280</dc:identifier>
<dc:source>The EMBO Journal 28, 3461 (2009)</dc:source>
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<title>Curved FtsZ protofilaments generate bending forces on liposome membranes</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/zM6wziIzknc/emboj.2009.277</link>
<description>We have created FtsZ-YFP-mts where an amphipathic helix on the C-terminus tethers FtsZ to the membrane. When incorporated inside multi-lamellar tubular liposomes, FtsZ-YFP-mts can assemble Z rings that generate a constriction force. When added to the outside of liposomes, FtsZ-YFP-mts bound and produced concave depressions, </description>
<content:encoded><![CDATA[

<p>
<b>Curved FtsZ protofilaments generate bending forces on liposome membranes</b>
</p>
<p>The EMBO Journal 28, 3476 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.277">doi:10.1038/emboj.2009.277</a>
</p>
<p>Authors: Masaki Osawa, David E Anderson &amp; Harold P Erickson</p>
<p>We have created FtsZ-YFP-mts where an amphipathic helix on the C-terminus tethers FtsZ to the membrane. When incorporated inside multi-lamellar tubular liposomes, FtsZ-YFP-mts can assemble Z rings that generate a constriction force. When added to the outside of liposomes, FtsZ-YFP-mts bound and produced concave depressions, </p>
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<dc:title>Curved FtsZ protofilaments generate bending forces on liposome membranes</dc:title>
<dc:creator>Masaki Osawa</dc:creator>
<dc:creator>David E Anderson</dc:creator>
<dc:creator>Harold P Erickson</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.277</dc:identifier>
<dc:source>The EMBO Journal 28, 3476 (2009)</dc:source>
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<title>Participation of Tom1L1 in EGF-stimulated endocytosis of EGF receptor</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/D7pqGzFLEKI/emboj.2009.282</link>
<description>Although many proteins have been shown to participate in ligand-stimulated endocytosis of EGF receptor (EGFR), the adaptor protein responsible for interaction of activated EGFR with endocytic machinery remains elusive. We show here that EGF stimulates transient tyrosine phosphorylation of Tom1L1 by the Src family kinases, </description>
<content:encoded><![CDATA[

<p>
<b>Participation of Tom1L1 in EGF-stimulated endocytosis of EGF receptor</b>
</p>
<p>The EMBO Journal 28, 3485 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.282">doi:10.1038/emboj.2009.282</a>
</p>
<p>Authors: Ning Sheng Liu, Li Shen Loo, Eva Loh, Li-Fong Seet &amp; Wanjin Hong</p>
<p>Although many proteins have been shown to participate in ligand-stimulated endocytosis of EGF receptor (EGFR), the adaptor protein responsible for interaction of activated EGFR with endocytic machinery remains elusive. We show here that EGF stimulates transient tyrosine phosphorylation of Tom1L1 by the Src family kinases, </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/D7pqGzFLEKI" height="1" width="1"/>]]></content:encoded>
<dc:title>Participation of Tom1L1 in EGF-stimulated endocytosis of EGF receptor</dc:title>
<dc:creator>Ning Sheng Liu</dc:creator>
<dc:creator>Li Shen Loo</dc:creator>
<dc:creator>Eva Loh</dc:creator>
<dc:creator>Li-Fong Seet</dc:creator>
<dc:creator>Wanjin Hong</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.282</dc:identifier>
<dc:source>The EMBO Journal 28, 3485 (2009)</dc:source>
<dc:date>2009-10-01</dc:date>
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<title>SnoN functions as a tumour suppressor by inducing premature senescence</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/plh-CDKJV2M/emboj.2009.250</link>
<description>SnoN represses TGF-β signalling to promote cell proliferation and has been defined as a proto-oncogene partly due to its elevated expression in many human cancer cells. Although the anti-tumourigenic activity of SnoN has been suggested, the molecular basis for this has not been defined. We </description>
<content:encoded><![CDATA[

<p>
<b>SnoN functions as a tumour suppressor by inducing premature senescence</b>
</p>
<p>The EMBO Journal 28, 3500 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.250">doi:10.1038/emboj.2009.250</a>
</p>
<p>Authors: Deng Pan, Qingwei Zhu &amp; Kunxin Luo</p>
<p>SnoN represses TGF-&#946; signalling to promote cell proliferation and has been defined as a proto-oncogene partly due to its elevated expression in many human cancer cells. Although the anti-tumourigenic activity of SnoN has been suggested, the molecular basis for this has not been defined. We </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/plh-CDKJV2M" height="1" width="1"/>]]></content:encoded>
<dc:title>SnoN functions as a tumour suppressor by inducing premature senescence</dc:title>
<dc:creator>Deng Pan</dc:creator>
<dc:creator>Qingwei Zhu</dc:creator>
<dc:creator>Kunxin Luo</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.250</dc:identifier>
<dc:source>The EMBO Journal 28, 3500 (2009)</dc:source>
<dc:date>2009-09-10</dc:date>
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<prism:publicationDate>2009-09-10</prism:publicationDate>
<prism:doi>10.1038/emboj.2009.250</prism:doi>
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<title>4E-BP1 is a target of Smad4 essential for TGFβ-mediated inhibition of cell proliferation</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/-4wleS5rywg/emboj.2009.291</link>
<description>Assembly of the multi-subunit eukaryotic translation initiation factor-4F (eIF4F) is critical for protein synthesis and cell growth and proliferation. eIF4F formation is regulated by the translation-inhibitory protein 4E-BP1. While proliferation factors and intracellular pathways that impinge upon 4E-BP1 phosphorylation have been extensively studied, how they </description>
<content:encoded><![CDATA[

<p>
<b>4E-BP1 is a target of Smad4 essential for TGF&#946;-mediated inhibition of cell proliferation</b>
</p>
<p>The EMBO Journal 28, 3514 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.291">doi:10.1038/emboj.2009.291</a>
</p>
<p>Authors: Rania Azar, Amandine Alard, Christiane Susini, Corinne Bousquet &amp; St&#233;phane Pyronnet</p>
<p>Assembly of the multi-subunit eukaryotic translation initiation factor-4F (eIF4F) is critical for protein synthesis and cell growth and proliferation. eIF4F formation is regulated by the translation-inhibitory protein 4E-BP1. While proliferation factors and intracellular pathways that impinge upon 4E-BP1 phosphorylation have been extensively studied, how they </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/-4wleS5rywg" height="1" width="1"/>]]></content:encoded>
<dc:title>4E-BP1 is a target of Smad4 essential for TGFβ-mediated inhibition of cell proliferation</dc:title>
<dc:creator>Rania Azar</dc:creator>
<dc:creator>Amandine Alard</dc:creator>
<dc:creator>Christiane Susini</dc:creator>
<dc:creator>Corinne Bousquet</dc:creator>
<dc:creator>Stéphane Pyronnet</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.291</dc:identifier>
<dc:source>The EMBO Journal 28, 3514 (2009)</dc:source>
<dc:date>2009-10-15</dc:date>
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<title>RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/fQiWnvXbdpc/emboj.2009.283</link>
<description>In contrast to Escherichia coli, initiation of mRNA decay in Gram-positive organisms is poorly understood. We studied the fate of the highly structured RNAs generated by premature transcription termination of S-adenosylmethionine (SAM)-dependent riboswitches in Bacillus subtilis. An essential protein of earlier unknown </description>
<content:encoded><![CDATA[

<p>
<b>RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis</b>
</p>
<p>The EMBO Journal 28, 3523 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.283">doi:10.1038/emboj.2009.283</a>
</p>
<p>Authors: Karen Shahbabian, Ailar Jamalli, L&#233;na Zig &amp; Harald Putzer</p>
<p>In contrast to Escherichia coli, initiation of mRNA decay in Gram-positive organisms is poorly understood. We studied the fate of the highly structured RNAs generated by premature transcription termination of S-adenosylmethionine (SAM)-dependent riboswitches in Bacillus subtilis. An essential protein of earlier unknown </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/fQiWnvXbdpc" height="1" width="1"/>]]></content:encoded>
<dc:title>RNase Y, a novel endoribonuclease, initiates riboswitch turnover in Bacillus subtilis</dc:title>
<dc:creator>Karen Shahbabian</dc:creator>
<dc:creator>Ailar Jamalli</dc:creator>
<dc:creator>Léna Zig</dc:creator>
<dc:creator>Harald Putzer</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.283</dc:identifier>
<dc:source>The EMBO Journal 28, 3523 (2009)</dc:source>
<dc:date>2009-09-24</dc:date>
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<title>PARP-1 transcriptional activity is regulated by sumoylation upon heat shock</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/cG4k8GYr08M/emboj.2009.279</link>
<description>Heat shock and other environmental stresses rapidly induce transcriptional responses subject to regulation by a variety of post-translational modifications. Among these, poly(ADP-ribosyl)ation and sumoylation have received growing attention. Here we show that the SUMO E3 ligase PIASy interacts with the poly(ADP-ribose) polymerase PARP-1, and that </description>
<content:encoded><![CDATA[

<p>
<b>PARP-1 transcriptional activity is regulated by sumoylation upon heat shock</b>
</p>
<p>The EMBO Journal 28, 3534 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.279">doi:10.1038/emboj.2009.279</a>
</p>
<p>Authors: Nadine Martin, Klaus Schwamborn, Val&#233;rie Schreiber, Andreas Werner, Christelle Guillier, Xiang-Dong Zhang, Oliver Bischof, Jacob-S Seeler &amp; Anne Dejean</p>
<p>Heat shock and other environmental stresses rapidly induce transcriptional responses subject to regulation by a variety of post-translational modifications. Among these, poly(ADP-ribosyl)ation and sumoylation have received growing attention. Here we show that the SUMO E3 ligase PIASy interacts with the poly(ADP-ribose) polymerase PARP-1, and that </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/cG4k8GYr08M" height="1" width="1"/>]]></content:encoded>
<dc:title>PARP-1 transcriptional activity is regulated by sumoylation upon heat shock</dc:title>
<dc:creator>Nadine Martin</dc:creator>
<dc:creator>Klaus Schwamborn</dc:creator>
<dc:creator>Valérie Schreiber</dc:creator>
<dc:creator>Andreas Werner</dc:creator>
<dc:creator>Christelle Guillier</dc:creator>
<dc:creator>Xiang-Dong Zhang</dc:creator>
<dc:creator>Oliver Bischof</dc:creator>
<dc:creator>Jacob-S Seeler</dc:creator>
<dc:creator>Anne Dejean</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.279</dc:identifier>
<dc:source>The EMBO Journal 28, 3534 (2009)</dc:source>
<dc:date>2009-09-24</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2009-09-24</prism:publicationDate>
<prism:doi>10.1038/emboj.2009.279</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2009.279</prism:url>
<prism:volume>28</prism:volume>
<prism:number>22</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>3534</prism:startingPage>
<prism:endingPage>3548</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2009.279</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2009.278">
<title>The MRT-1 nuclease is required for DNA crosslink repair and telomerase activity in vivo in Caenorhabditis elegans</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/zeiesKVrqIo/emboj.2009.278</link>
<description>The telomerase reverse transcriptase adds de novo DNA repeats to chromosome termini. Here we define Caenorhabditis elegans MRT-1 as a novel factor required for telomerase-mediated telomere replication and the DNA-damage response. MRT-1 is composed of an N-terminal domain homologous to the second OB-fold </description>
<content:encoded><![CDATA[

<p>
<b>The MRT-1 nuclease is required for DNA crosslink repair and telomerase activity in vivo in Caenorhabditis elegans</b>
</p>
<p>The EMBO Journal 28, 3549 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.278">doi:10.1038/emboj.2009.278</a>
</p>
<p>Authors: Bettina Meier, Louise J Barber, Yan Liu, Ludmila Shtessel, Simon J Boulton, Anton Gartner &amp; Shawn Ahmed</p>
<p>The telomerase reverse transcriptase adds de novo DNA repeats to chromosome termini. Here we define Caenorhabditis elegans MRT-1 as a novel factor required for telomerase-mediated telomere replication and the DNA-damage response. MRT-1 is composed of an N-terminal domain homologous to the second OB-fold </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/zeiesKVrqIo" height="1" width="1"/>]]></content:encoded>
<dc:title>The MRT-1 nuclease is required for DNA crosslink repair and telomerase activity in vivo in Caenorhabditis elegans</dc:title>
<dc:creator>Bettina Meier</dc:creator>
<dc:creator>Louise J Barber</dc:creator>
<dc:creator>Yan Liu</dc:creator>
<dc:creator>Ludmila Shtessel</dc:creator>
<dc:creator>Simon J Boulton</dc:creator>
<dc:creator>Anton Gartner</dc:creator>
<dc:creator>Shawn Ahmed</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.278</dc:identifier>
<dc:source>The EMBO Journal 28, 3549 (2009)</dc:source>
<dc:date>2009-09-24</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2009-09-24</prism:publicationDate>
<prism:doi>10.1038/emboj.2009.278</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2009.278</prism:url>
<prism:volume>28</prism:volume>
<prism:number>22</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>3549</prism:startingPage>
<prism:endingPage>3563</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2009.278</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2009.289">
<title>Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/1yG_3wtUulY/emboj.2009.289</link>
<description>The receptor-type protein tyrosine phosphatases (RPTPs) have been linked to signal transduction, cell adhesion, and neurite extension. PTPRT/RPTPρ is exclusively expressed in the central nervous system and regulates synapse formation by interacting with cell adhesion molecules and Fyn protein tyrosine kinase. Overexpression of PTPRT in </description>
<content:encoded><![CDATA[

<p>
<b>Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn</b>
</p>
<p>The EMBO Journal 28, 3564 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.289">doi:10.1038/emboj.2009.289</a>
</p>
<p>Authors: So-Hee Lim, Seok-Kyu Kwon, Myung Kyu Lee, Jeonghee Moon, Dae Gwin Jeong, Eunha Park, Seung Jun Kim, Byung Chul Park, Sang Chul Lee, Seong-Eon Ryu, Dae-Yeul Yu, Bong Hyun Chung, Eunjoon Kim, Pyung-Keun Myung &amp; Jae-Ran Lee</p>
<p>The receptor-type protein tyrosine phosphatases (RPTPs) have been linked to signal transduction, cell adhesion, and neurite extension. PTPRT/RPTP&#961; is exclusively expressed in the central nervous system and regulates synapse formation by interacting with cell adhesion molecules and Fyn protein tyrosine kinase. Overexpression of PTPRT in </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/1yG_3wtUulY" height="1" width="1"/>]]></content:encoded>
<dc:title>Synapse formation regulated by protein tyrosine phosphatase receptor T through interaction with cell adhesion molecules and Fyn</dc:title>
<dc:creator>So-Hee Lim</dc:creator>
<dc:creator>Seok-Kyu Kwon</dc:creator>
<dc:creator>Myung Kyu Lee</dc:creator>
<dc:creator>Jeonghee Moon</dc:creator>
<dc:creator>Dae Gwin Jeong</dc:creator>
<dc:creator>Eunha Park</dc:creator>
<dc:creator>Seung Jun Kim</dc:creator>
<dc:creator>Byung Chul Park</dc:creator>
<dc:creator>Sang Chul Lee</dc:creator>
<dc:creator>Seong-Eon Ryu</dc:creator>
<dc:creator>Dae-Yeul Yu</dc:creator>
<dc:creator>Bong Hyun Chung</dc:creator>
<dc:creator>Eunjoon Kim</dc:creator>
<dc:creator>Pyung-Keun Myung</dc:creator>
<dc:creator>Jae-Ran Lee</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.289</dc:identifier>
<dc:source>The EMBO Journal 28, 3564 (2009)</dc:source>
<dc:date>2009-10-08</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2009-10-08</prism:publicationDate>
<prism:doi>10.1038/emboj.2009.289</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2009.289</prism:url>
<prism:volume>28</prism:volume>
<prism:number>22</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>3564</prism:startingPage>
<prism:endingPage>3578</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2009.289</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2009.286">
<title>Adaptability of the semi-invariant natural killer T-cell receptor towards structurally diverse CD1d-restricted ligands</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/mTQ0r9y6jqM/emboj.2009.286</link>
<description>The semi-invariant natural killer (NK) T-cell receptor (NKTcr) recognises structurally diverse glycolipid antigens presented by the monomorphic CD1d molecule. While the α-chain of the NKTcr is invariant, the β-chain is more diverse, but how this diversity enables the NKTcr to recognise diverse antigens, such as </description>
<content:encoded><![CDATA[

<p>
<b>Adaptability of the semi-invariant natural killer T-cell receptor towards structurally diverse CD1d-restricted ligands</b>
</p>
<p>The EMBO Journal 28, 3579 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.286">doi:10.1038/emboj.2009.286</a>
</p>
<p>Authors: William C Florence, Chengfeng Xia, Laura E Gordy, Wenlan Chen, Yalong Zhang, James Scott-Browne, Yuki Kinjo, Karl O A Yu, Santosh Keshipeddy, Daniel G Pellicci, Onisha Patel, Lars Kjer-Nielsen, James McCluskey, Dale I Godfrey, Jamie Rossjohn, Stewart K Richardson, Steven A Porcelli, Amy R Howell, Kyoko Hayakawa, Laurent Gapin, Dirk M Zajonc, Peng George Wang &amp; Sebastian Joyce</p>
<p>The semi-invariant natural killer (NK) T-cell receptor (NKTcr) recognises structurally diverse glycolipid antigens presented by the monomorphic CD1d molecule. While the &#945;-chain of the NKTcr is invariant, the &#946;-chain is more diverse, but how this diversity enables the NKTcr to recognise diverse antigens, such as </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/mTQ0r9y6jqM" height="1" width="1"/>]]></content:encoded>
<dc:title>Adaptability of the semi-invariant natural killer T-cell receptor towards structurally diverse CD1d-restricted ligands</dc:title>
<dc:creator>William C Florence</dc:creator>
<dc:creator>Chengfeng Xia</dc:creator>
<dc:creator>Laura E Gordy</dc:creator>
<dc:creator>Wenlan Chen</dc:creator>
<dc:creator>Yalong Zhang</dc:creator>
<dc:creator>James Scott-Browne</dc:creator>
<dc:creator>Yuki Kinjo</dc:creator>
<dc:creator>Karl O A Yu</dc:creator>
<dc:creator>Santosh Keshipeddy</dc:creator>
<dc:creator>Daniel G Pellicci</dc:creator>
<dc:creator>Onisha Patel</dc:creator>
<dc:creator>Lars Kjer-Nielsen</dc:creator>
<dc:creator>James McCluskey</dc:creator>
<dc:creator>Dale I Godfrey</dc:creator>
<dc:creator>Jamie Rossjohn</dc:creator>
<dc:creator>Stewart K Richardson</dc:creator>
<dc:creator>Steven A Porcelli</dc:creator>
<dc:creator>Amy R Howell</dc:creator>
<dc:creator>Kyoko Hayakawa</dc:creator>
<dc:creator>Laurent Gapin</dc:creator>
<dc:creator>Dirk M Zajonc</dc:creator>
<dc:creator>Peng George Wang</dc:creator>
<dc:creator>Sebastian Joyce</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.286</dc:identifier>
<dc:source>The EMBO Journal 28, 3579 (2009)</dc:source>
<dc:date>2009-10-08</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2009-10-08</prism:publicationDate>
<prism:doi>10.1038/emboj.2009.286</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2009.286</prism:url>
<prism:volume>28</prism:volume>
<prism:number>22</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>3579</prism:startingPage>
<prism:endingPage>3590</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2009.286</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2009.290">
<title>AP-2γ promotes proliferation in breast tumour cells by direct repression of the CDKN1A gene</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/qzoHh3ULI2Y/emboj.2009.290</link>
<description>Overexpression of the activator protein (AP)-2γ transcription factor in breast tumours has been identified as an independent predictor of poor outcome and failure of hormone therapy. To understand further the function of AP-2γ in breast carcinoma, we have used an RNA interference and gene expression </description>
<content:encoded><![CDATA[

<p>
<b>AP-2&#947; promotes proliferation in breast tumour cells by direct repression of the CDKN1A gene</b>
</p>
<p>The EMBO Journal 28, 3591 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.290">doi:10.1038/emboj.2009.290</a>
</p>
<p>Authors: Christopher M J Williams, Angelo G Scibetta, J Karsten Friedrich, Monica Canosa, Chiara Berlato, Charlotte H Moss &amp; Helen C Hurst</p>
<p>Overexpression of the activator protein (AP)-2&#947; transcription factor in breast tumours has been identified as an independent predictor of poor outcome and failure of hormone therapy. To understand further the function of AP-2&#947; in breast carcinoma, we have used an RNA interference and gene expression </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/qzoHh3ULI2Y" height="1" width="1"/>]]></content:encoded>
<dc:title>AP-2γ promotes proliferation in breast tumour cells by direct repression of the CDKN1A gene</dc:title>
<dc:creator>Christopher M J Williams</dc:creator>
<dc:creator>Angelo G Scibetta</dc:creator>
<dc:creator>J Karsten Friedrich</dc:creator>
<dc:creator>Monica Canosa</dc:creator>
<dc:creator>Chiara Berlato</dc:creator>
<dc:creator>Charlotte H Moss</dc:creator>
<dc:creator>Helen C Hurst</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.290</dc:identifier>
<dc:source>The EMBO Journal 28, 3591 (2009)</dc:source>
<dc:date>2009-10-01</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2009-10-01</prism:publicationDate>
<prism:doi>10.1038/emboj.2009.290</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2009.290</prism:url>
<prism:volume>28</prism:volume>
<prism:number>22</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>3591</prism:startingPage>
<prism:endingPage>3601</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2009.290</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2009.288">
<title>Mg2+-dependent gating of bacterial MgtE channel underlies Mg2+ homeostasis</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/0oRmS2VoC_o/emboj.2009.288</link>
<description>The MgtE family of Mg2+ transporters is ubiquitously distributed in all phylogenetic domains. Recent crystal structures of the full-length MgtE and of its cytosolic domain in the presence and absence of Mg2+ suggested a Mg2+-homeostasis mechanism, in which the </description>
<content:encoded><![CDATA[

<p>
<b>Mg2&#43;-dependent gating of bacterial MgtE channel underlies Mg2&#43; homeostasis</b>
</p>
<p>The EMBO Journal 28, 3602 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.288">doi:10.1038/emboj.2009.288</a>
</p>
<p>Authors: Motoyuki Hattori, Norihiko Iwase, Noritaka Furuya, Yoshiki Tanaka, Tomoya Tsukazaki, Ryuichiro Ishitani, Michael E Maguire, Koichi Ito, Andres Maturana &amp; Osamu Nureki</p>
<p>The MgtE family of Mg2&#43; transporters is ubiquitously distributed in all phylogenetic domains. Recent crystal structures of the full-length MgtE and of its cytosolic domain in the presence and absence of Mg2&#43; suggested a Mg2&#43;-homeostasis mechanism, in which the </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/0oRmS2VoC_o" height="1" width="1"/>]]></content:encoded>
<dc:title>Mg2+-dependent gating of bacterial MgtE channel underlies Mg2+ homeostasis</dc:title>
<dc:creator>Motoyuki Hattori</dc:creator>
<dc:creator>Norihiko Iwase</dc:creator>
<dc:creator>Noritaka Furuya</dc:creator>
<dc:creator>Yoshiki Tanaka</dc:creator>
<dc:creator>Tomoya Tsukazaki</dc:creator>
<dc:creator>Ryuichiro Ishitani</dc:creator>
<dc:creator>Michael E Maguire</dc:creator>
<dc:creator>Koichi Ito</dc:creator>
<dc:creator>Andres Maturana</dc:creator>
<dc:creator>Osamu Nureki</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.288</dc:identifier>
<dc:source>The EMBO Journal 28, 3602 (2009)</dc:source>
<dc:date>2009-10-01</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2009-10-01</prism:publicationDate>
<prism:doi>10.1038/emboj.2009.288</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2009.288</prism:url>
<prism:volume>28</prism:volume>
<prism:number>22</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>3602</prism:startingPage>
<prism:endingPage>3612</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2009.288</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2009.284">
<title>Structural basis of phosphodiesterase 6 inhibition by the C-terminal region of the γ-subunit</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/faSmSBJlOAI/emboj.2009.284</link>
<description>The inhibitory interaction of phosphodiesterase-6 (PDE6) with its γ-subunit (Pγ) is pivotal in vertebrate phototransduction. Here, crystal structures of a chimaeric PDE5/PDE6 catalytic domain (PDE5/6cd) complexed with sildenafil or 3-isobutyl-1-methylxanthine and the Pγ-inhibitory peptide Pγ70−87 have been determined at 2.9 and 3.0 Å, </description>
<content:encoded><![CDATA[

<p>
<b>Structural basis of phosphodiesterase 6 inhibition by the C-terminal region of the &#947;-subunit</b>
</p>
<p>The EMBO Journal 28, 3613 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.284">doi:10.1038/emboj.2009.284</a>
</p>
<p>Authors: Brandy Barren, Lokesh Gakhar, Hakim Muradov, Kimberly K Boyd, S Ramaswamy &amp; Nikolai O Artemyev</p>
<p>The inhibitory interaction of phosphodiesterase-6 (PDE6) with its &#947;-subunit (P&#947;) is pivotal in vertebrate phototransduction. Here, crystal structures of a chimaeric PDE5/PDE6 catalytic domain (PDE5/6cd) complexed with sildenafil or 3-isobutyl-1-methylxanthine and the P&#947;-inhibitory peptide P&#947;70&#8722;87 have been determined at 2.9 and 3.0 &#197;, </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/faSmSBJlOAI" height="1" width="1"/>]]></content:encoded>
<dc:title>Structural basis of phosphodiesterase 6 inhibition by the C-terminal region of the γ-subunit</dc:title>
<dc:creator>Brandy Barren</dc:creator>
<dc:creator>Lokesh Gakhar</dc:creator>
<dc:creator>Hakim Muradov</dc:creator>
<dc:creator>Kimberly K Boyd</dc:creator>
<dc:creator>S Ramaswamy</dc:creator>
<dc:creator>Nikolai O Artemyev</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.284</dc:identifier>
<dc:source>The EMBO Journal 28, 3613 (2009)</dc:source>
<dc:date>2009-10-01</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2009-10-01</prism:publicationDate>
<prism:doi>10.1038/emboj.2009.284</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2009.284</prism:url>
<prism:volume>28</prism:volume>
<prism:number>22</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>3613</prism:startingPage>
<prism:endingPage>3622</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2009.284</feedburner:origLink></item>
<item rdf:about="http://dx.doi.org/10.1038/emboj.2009.287">
<title>The structure of an integrin/talin complex reveals the basis of inside-out signal transduction</title>
<link>http://feeds.nature.com/~r/emboj/rss/current/~3/69VU0veKPdQ/emboj.2009.287</link>
<description>Fundamental to cell adhesion and migration, integrins are large heterodimeric membrane proteins that uniquely mediate inside-out signal transduction, whereby adhesion to the extracellular matrix is activated from within the cell by direct binding of talin to the cytoplasmic tail of the β integrin subunit. Here, </description>
<content:encoded><![CDATA[

<p>
<b>The structure of an integrin/talin complex reveals the basis of inside-out signal transduction</b>
</p>
<p>The EMBO Journal 28, 3623 (2009). <a href="http://dx.doi.org/10.1038/emboj.2009.287">doi:10.1038/emboj.2009.287</a>
</p>
<p>Authors: Nicholas J Anthis, Kate L Wegener, Feng Ye, Chungho Kim, Benjamin T Goult, Edward D Lowe, Ioannis Vakonakis, Neil Bate, David R Critchley, Mark H Ginsberg &amp; Iain D Campbell</p>
<p>Fundamental to cell adhesion and migration, integrins are large heterodimeric membrane proteins that uniquely mediate inside-out signal transduction, whereby adhesion to the extracellular matrix is activated from within the cell by direct binding of talin to the cytoplasmic tail of the &#946; integrin subunit. Here, </p>
<img src="http://feeds.feedburner.com/~r/emboj/rss/current/~4/69VU0veKPdQ" height="1" width="1"/>]]></content:encoded>
<dc:title>The structure of an integrin/talin complex reveals the basis of inside-out signal transduction</dc:title>
<dc:creator>Nicholas J Anthis</dc:creator>
<dc:creator>Kate L Wegener</dc:creator>
<dc:creator>Feng Ye</dc:creator>
<dc:creator>Chungho Kim</dc:creator>
<dc:creator>Benjamin T Goult</dc:creator>
<dc:creator>Edward D Lowe</dc:creator>
<dc:creator>Ioannis Vakonakis</dc:creator>
<dc:creator>Neil Bate</dc:creator>
<dc:creator>David R Critchley</dc:creator>
<dc:creator>Mark H Ginsberg</dc:creator>
<dc:creator>Iain D Campbell</dc:creator>
<dc:identifier>doi:10.1038/emboj.2009.287</dc:identifier>
<dc:source>The EMBO Journal 28, 3623 (2009)</dc:source>
<dc:date>2009-10-01</dc:date>
<prism:publicationName>The EMBO Journal</prism:publicationName>
<prism:publicationDate>2009-10-01</prism:publicationDate>
<prism:doi>10.1038/emboj.2009.287</prism:doi>
<prism:url>http://dx.doi.org/10.1038/emboj.2009.287</prism:url>
<prism:volume>28</prism:volume>
<prism:number>22</prism:number>
<prism:section>Article</prism:section>
<prism:startingPage>3623</prism:startingPage>
<prism:endingPage>3632</prism:endingPage>
<feedburner:origLink>http://dx.doi.org/10.1038/emboj.2009.287</feedburner:origLink></item>
</rdf:RDF>
