Journal
STRUCTURE
Volume 24, Issue 7, Pages 1130-1141Publisher
CELL PRESS
DOI: 10.1016/j.str.2016.04.016
Keywords
-
Funding
- Biotechnology and Biological Sciences Research Council (BBSRC) DTP fellowship
- BBSRC [BB/N007336/1]
- Wellcome Trust [088785/Z/09/Z]
- BBSRC DTP studentship
- BBSRC [BB/N007336/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [1627291, BB/N007336/1] Funding Source: researchfish
Ask authors/readers for more resources
Cell migration requires coordination between integrin-mediated cell adhesion to the extracellular matrix and force applied to adhesion sites. Talin plays a key role in coupling integrin receptors to the actomyosin contractile machinery, while deleted in liver cancer 1 (DLC1) is a Rho GAP that binds talin and regulates Rho, and therefore actomyosin contractility. We show that the LD motif of DLC1 forms a helix that binds to the four-helix bundle of the talin R8 domain in a canonical triple-helix arrangement. We demonstrate that the same R8 surface interacts with the paxillin LD1 and LD2 motifs. We identify key charged residues that stabilize the R8 interactions with LD motifs and demonstrate their importance in vitro and in cells. Our results suggest a network of competitive interactions in adhesion complexes that involve LD motifs, and identify mutations that can be used to analyze the biological roles of specific protein-protein interactions in cell migration.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available