Mena binds α5 integrin directly and modulates α5β1 function
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; ... Show more Show less
DownloadGupton-2012-Mena binds alpha 5 i.pdf (5.183Mb)
PUBLISHER_CC
Publisher with Creative Commons License
Creative Commons Attribution
Terms of use
Metadata
Show full item recordAbstract
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.
Date issued
2012-08Department
Massachusetts Institute of Technology. Department of Biological Engineering; Massachusetts Institute of Technology. Department of Biology; Koch Institute for Integrative Cancer Research at MITJournal
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
ISSN
0021-9525
1540-8140