The EMBO Journal 28, 3277 (2009). doi:10.1038/emboj.2009.299

Authors: Jessica Greenwood & Julia Promisel Cooper

EMBO J2821, 3390–3399 (2009); published online 17 September 2009The prevention of nonhomologous end-joining (NHEJ) reactions between chromosome ends is crucial for maintaining genome stability. Although this protective function is known to be fulfilled by a core of conserved telomeric proteins that are collectively known as Shelterin, its mechanistic details remain a mystery. In this issue, Sarthy et al (2009) lend fresh insight by developing an ingenious method to dissect the role of hRAP1 in preventing telomeric NHEJ independently of other Shelterin components.

The EMBO Journal 28, 3279 (2009). doi:10.1038/emboj.2009.269

Authors: Kazuhito V Tabata, Ken Sato, Toru Ide, Takayuki Nishizaka, Akihiko Nakano & Hiroyuki Noji

Selective protein export from the endoplasmic reticulum is mediated by COPII vesicles. Here, we investigated the dynamics of fluorescently labelled cargo and non-cargo proteins during COPII vesicle formation using single-molecule microscopy combined with an artificial planar lipid bilayer. Single-molecule analysis showed that the Sar1p–Sec23/24p-cargo complex,

The EMBO Journal 28, 3290 (2009). doi:10.1038/emboj.2009.272

Authors: Anbing Shi, Lin Sun, Riju Banerjee, Michael Tobin, Yinhua Zhang & Barth D Grant

After endocytosis, most cargo enters the pleiomorphic early endosomes in which sorting occurs. As endosomes mature, transmembrane cargo can be sequestered into inwardly budding vesicles for degradation, or can exit the endosome in membrane tubules for recycling to the plasma membrane, the recycling endosome, or

The EMBO Journal 28, 3303 (2009). doi:10.1038/emboj.2009.261

Authors: Vikram K Bhatia, Kenneth L Madsen, Pierre-Yves Bolinger, Andreas Kunding, Per Hedegård, Ulrik Gether & Dimitrios Stamou

BAR (Bin/Amphiphysin/Rvs) domains and amphipathic α-helices (AHs) are believed to be sensors of membrane curvature thus facilitating the assembly of protein complexes on curved membranes. Here, we used quantitative fluorescence microscopy to compare the binding of both motifs on single nanosized liposomes of different diameters

The EMBO Journal 28, 3315 (2009). doi:10.1038/emboj.2009.267

Authors: Juan José Fung, Xavier Deupi, Leonardo Pardo, Xiao Jie Yao, Gisselle A Velez-Ruiz, Brian T DeVree, Roger K Sunahara & Brian K Kobilka

The β2-adrenoceptor (β2AR) was one of the first Family A G protein-coupled receptors (GPCRs) shown to form oligomers in cellular membranes, yet we still know little about the number and arrangement of protomers in oligomers, the influence of ligands on the

The EMBO Journal 28, 3329 (2009). doi:10.1038/emboj.2009.285

Authors: Tokameh Mahmoudi, Vivian S W Li, Ser Sue Ng, Nadia Taouatas, Robert G J Vries, Shabaz Mohammed, Albert J Heck & Hans Clevers

Wnt signalling maintains the undifferentiated state of intestinal crypt/progenitor cells through the TCF4/β-catenin-activating transcriptional complex. In colorectal cancer, activating mutations in Wnt pathway components lead to inappropriate activation of the TCF4/β-catenin transcriptional programme and tumourigenesis. The mechanisms by which TCF4/β-catenin activate key target genes are

The EMBO Journal 28, 3341 (2009). doi:10.1038/emboj.2009.271

Authors: Francesca De Santa, Vipin Narang, Zhei Hwee Yap, Betsabeh Khoramian Tusi, Thomas Burgold, Liv Austenaa, Gabriele Bucci, Marieta Caganova, Samuele Notarbartolo, Stefano Casola, Giuseppe Testa, Wing-Kin Sung, Chia-Lin Wei & Gioacchino Natoli

Jmjd3, a JmjC family histone demethylase, is induced by the transcription factor NF-kB in response to microbial stimuli. Jmjd3 erases H3K27me3, a histone mark associated with transcriptional repression and involved in lineage determination. However, the specific contribution of Jmjd3 induction and H3K27me3 demethylation to inflammatory

The EMBO Journal 28, 3353 (2009). doi:10.1038/emboj.2009.260

Authors: Yukimatsu Toh, Daijiro Takeshita, Tomoyuki Numata, Shuya Fukai, Osamu Nureki & Kozo Tomita

The CCA-adding enzyme synthesizes the CCA sequence at the 3′ end of tRNA without a nucleic acid template. The crystal structures of class II Thermotoga maritima CCA-adding enzyme and its complexes with CTP or ATP were determined. The structure-based replacement of both the catalytic

The EMBO Journal 28, 3366 (2009). doi:10.1038/emboj.2009.268

Authors: Yuan Liu, Satoru Mimura, Tsutomu Kishi & Takumi Kamura

SCF-type E3-ubiquitin ligases control numerous cellular processes through the ubiquitin-proteasome pathway. However, the regulation of SCF function remains largely uncharacterized. Here, we report a novel SCF complex-interacting protein, Lag2, in Saccharomyces cerevisiae. Lag2 interacts with the SCF complex under physiological conditions. Lag2 negatively controls

The EMBO Journal 28, 3378 (2009). doi:10.1038/emboj.2009.270

Authors: Shinya Takahata, Yaxin Yu & David J Stillman

Regulation of the CLN1 and CLN2 G1 cyclin genes controls cell cycle progression. The SBF activator binds to these promoters but is kept inactive by the Whi5 and Stb1 inhibitors. The Cdc28 cyclin-dependent kinase phosphorylates Whi5, ending the inhibition. Our chromatin immunoprecipitation (ChIP)

The EMBO Journal 28, 3390 (2009). doi:10.1038/emboj.2009.275

Authors: Jay Sarthy, Nancy S Bae, Jonathan Scrafford & Peter Baumann

Telomeres, the nucleoprotein structures at the ends of linear chromosomes, promote genome stability by distinguishing chromosome termini from DNA double-strand breaks (DSBs). Cells possess two principal pathways for DSB repair: homologous recombination and non-homologous end joining (NHEJ). Several studies have implicated TRF2 in the protection

The EMBO Journal 28, 3400 (2009). doi:10.1038/emboj.2009.265

Authors: Helen Tinline-Purvis, Andrew P Savory, Jason K Cullen, Anoushka Davé, Jennifer Moss, Wendy L Bridge, Samuel Marguerat, Jürg Bähler, Jiannis Ragoussis, Richard Mott, Carol A Walker & Timothy C Humphrey

Loss of heterozygosity (LOH), a causal event in cancer and human genetic diseases, frequently encompasses multiple genetic loci and whole chromosome arms. However, the mechanisms by which such extensive LOH arises, and how it is suppressed in normal cells is poorly understood. We have developed

The EMBO Journal 28, 3413 (2009). doi:10.1038/emboj.2009.276

Authors: Andrea Beucher, Julie Birraux, Leopoldine Tchouandong, Olivia Barton, Atsushi Shibata, Sandro Conrad, Aaron A Goodarzi, Andrea Krempler, Penny A Jeggo & Markus Löbrich

Homologous recombination (HR) and non-homologous end joining (NHEJ) represent distinct pathways for repairing DNA double-strand breaks (DSBs). Previous work implicated Artemis and ATM in an NHEJ-dependent process, which repairs a defined subset of radiation-induced DSBs in G1-phase. Here, we show that in G2, as in

The EMBO Journal 28, 3428 (2009). doi:10.1038/emboj.2009.262

Authors: Vladimir Nekrasov, Jing Li, Martine Batoux, Milena Roux, Zhao-Hui Chu, Severine Lacombe, Alejandra Rougon, Pascal Bittel, Marta Kiss-Papp, Delphine Chinchilla, H Peter van Esse, Lucia Jorda, Benjamin Schwessinger, Valerie Nicaise, Bart P H J Thomma, Antonio Molina, Jonathan D G Jones & Cyril Zipfel

In plant innate immunity, the surface-exposed leucine-rich repeat receptor kinases EFR and FLS2 mediate recognition of the bacterial pathogen-associated molecular patterns EF-Tu and flagellin, respectively. We identified the Arabidopsis stromal-derived factor-2 (SDF2) as being required for EFR function, and to a lesser extent FLS2 function.

The EMBO Journal 28, 3439 (2009). doi:10.1038/emboj.2009.263

Authors: Yusuke Saijo, Nico Tintor, Xunli Lu, Philipp Rauf, Karolina Pajerowska-Mukhtar, Heidrun Häweker, Xinnian Dong, Silke Robatzek & Paul Schulze-Lefert

Pattern recognition receptors in eukaryotes initiate defence responses on detection of microbe-associated molecular patterns shared by many microbe species. The Leu-rich repeat receptor-like kinases FLS2 and EFR recognize the bacterial epitopes flg22 and elf18, derived from flagellin and elongation factor-Tu, respectively. We describe Arabidopsis ‘

The EMBO Journal 28, 3450 (2009). doi:10.1038/emboj.2009.274

Authors: Jordi Querol-Audí, Arnau Casañas, Isabel Usón, Daniel Luque, José R Castón, Ignasi Fita & Nuria Verdaguer

Vaults are ubiquitous ribonucleoprotein complexes involved in a diversity of cellular processes, including multidrug resistance, transport mechanisms and signal transmission. The vault particle shows a barrel-shaped structure organized in two identical moieties, each consisting of 39 copies of the major vault protein MVP. Earlier data

The EMBO Journal 28, 3458 (2009). doi:10.1038/emboj.2009.315

Authors: Nelson C Lau, Toshiro Ohsumi, Mark Borowsky, Robert E Kingston & Michael D Blower

Correction to: Xenopus