Mena binds α5 integrin directly and modulates α5β1 function
Name
Gupton-2012-Mena binds alpha 5 i.pdf
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5.18 MB
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Author(s)
Gupton, Stephanie L.
Riquelme, Daisy Noelia
Hughes-Alford, Shannon Kay
Tadros, Jenny
Rudina, Shireen S.
Hynes, Richard O.
Lauffenburger, Douglas A.
Gertler, Frank
Date Issued
August 2012
Journal
Journal of Cell Biology
Publisher
Rockefeller University Press, The
Citation
Gupton, S. L. et al. “Mena binds α5 integrin directly and modulates α5β1 function.” The Journal of Cell Biology 198.4 (2012): 657–676. © 2012 by The Rockefeller University Press
Version
Final published version
Abstract
Mena is an Ena/VASP family actin regulator with roles in cell migration, chemotaxis, cell–cell adhesion, tumor cell invasion, and metastasis. Although enriched in focal adhesions, Mena has no established function within these structures. We find that Mena forms an adhesion-regulated complex with α5β1 integrin, a fibronectin receptor involved in cell adhesion, motility, fibronectin fibrillogenesis, signaling, and growth factor receptor trafficking. Mena bound directly to the carboxy-terminal portion of the α5 cytoplasmic tail via a 91-residue region containing 13 five-residue “LERER” repeats. In fibroblasts, the Mena–α5 complex was required for “outside-in” α5β1 functions, including normal phosphorylation of FAK and paxillin and formation of fibrillar adhesions. It also supported fibrillogenesis and cell spreading and controlled cell migration speed. Thus, fibroblasts require Mena for multiple α5β1-dependent processes involving bidirectional interactions between the extracellular matrix and cytoplasmic focal adhesion proteins.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
Massachusetts Institute of Technology. Department of Biology
Koch Institute for Integrative Cancer Research at MIT
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Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported
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DOI of Published Version
https://doi.org/10.1083/jcb.201202079
