Featured
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Article |
MAP4K4 regulates integrin-FERM binding to control endothelial cell motility
A new MAP4K4–moesin–talin–β1-integrin pathway regulating endothelial cell motility was discovered through chemical and siRNA screens; loss of Map4k4 or inhibition of MAP4K4 kinase activity altered the sprout morphology of endothelial cells during angiogenesis by blocking moesin phosphorylation, which regulates the disassembly of focal adhesions, demonstrating that this pathway is involved in both normal and pathological angiogenesis.
- Philip Vitorino
- , Stacey Yeung
- & Weilan Ye
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Letter |
Nanoscale architecture of integrin-based cell adhesions
Focal adhesions link the extracellular matrix by integrin receptors to cytoplasmic actin filaments and are fundamental to human physiology. These authors determine the molecular architecture of focal adhesions by mapping protein organization at the nanoscale level. The results demonstrate that focal adhesions possess a well-organized ultrastructure made up of at least three spatial and functional compartments that mediate their interdependent functions.
- Pakorn Kanchanawong
- , Gleb Shtengel
- & Clare M. Waterman
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Letter |
Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics
The ability of cells to respond to physical forces is central to development and physiology, but until now it has been difficult to directly measure forces across proteins in vivo. Here, however, a calibrated biosensor is described that can measure forces with high sensitivity across specific proteins in cells. This is applied to the vinculin protein, and a regulatory mechanism is revealed in which the force applied to vinculin determines whether focal adhesions assemble or disassemble.
- Carsten Grashoff
- , Brenton D. Hoffman
- & Martin A. Schwartz
Force loading explains spatial sensing of ligands by cells