4f7g

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f7g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f7g OCA], [https://pdbe.org/4f7g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f7g RCSB], [https://www.ebi.ac.uk/pdbsum/4f7g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f7g ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

The activation of heterodimeric (alpha/beta) integrin transmembrane receptors by cytosolic protein talin is crucial for regulating diverse cell-adhesion-dependent processes, including blood coagulation, tissue remodeling, and cancer metastasis. This process is triggered by the coincident binding of N-terminal FERM (four-point-one-protein/ezrin/radixin/moesin) domain of talin (talin-FERM) to the inner membrane surface and integrin beta cytoplasmic tail, but how these binding events are spatiotemporally regulated remains obscure. Here we report the crystal structure of a dormant talin, revealing how a C-terminal talin rod segment (talin-RS) self-masks a key integrin-binding site on talin-FERM via a large interface. Unexpectedly, the structure also reveals a distinct negatively charged surface on talin-RS that electrostatically hinders the talin-FERM binding to the membrane. Such a dual inhibitory topology for talin is consistent with the biochemical and functional data, but differs significantly from a previous model. We show that upon enrichment with phosphotidylinositol-4,5-bisphosphate (PIP2) - a known talin activator, membrane strongly attracts a positively charged surface on talin-FERM and simultaneously repels the negatively charged surface on talin-RS. Such an electrostatic "pull-push" process promotes the relief of the dual inhibition of talin-FERM, which differs from the classic "steric clash" model for conventional PIP2-induced FERM domain activation. These data therefore unravel a new type of membrane-dependent FERM domain regulation and illustrate how it mediates the talin on/off switches to regulate integrin transmembrane signaling and cell adhesion.Cell Research advance online publication 19 June 2012; doi:10.1038/cr.2012.97.

A novel membrane-dependent on/off switch mechanism of talin FERM domain at sites of cell adhesion.,Song X, Yang J, Hirbawi J, Ye S, Perera HD, Goksoy E, Dwivedi P, Plow EF, Zhang R, Qin J Cell Res. 2012 Jun 19. doi: 10.1038/cr.2012.97. PMID:22710802<ref>PMID:22710802</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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*[[Talin|Talin]]