Two Distinct Head-Tail Interfaces Cooperate to Suppress Activation of Vinculin by Talin
Open Access
- 1 April 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (17) , 17109-17117
- https://doi.org/10.1074/jbc.m414704200
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- Characterization of an Actin-binding Site within the Talin FERM DomainJournal of Molecular Biology, 2004
- Crystal Structure of Human VinculinStructure, 2004
- Structural basis for vinculin activation at sites of cell adhesionNature, 2004
- Vinculin activation by talin through helical bundle conversionNature, 2003
- Intact Vinculin Protein Is Required for Control of Cell Shape, Cell Mechanics, and rac-Dependent Lamellipodia FormationBiochemical and Biophysical Research Communications, 2002
- Integration of Multiple Signals Through Cooperative Regulation of the N-WASP-Arp2/3 ComplexScience, 2000
- A Conserved Motif in the Tail Domain of Vinculin Mediates Association with and Insertion into Acidic Phospholipid BilayersBiochemistry, 1998
- F-actin binding site masked by the intramolecular association of vinculin head and tail domainsNature, 1995
- Vinculin is essential for muscle function in the nematode.The Journal of cell biology, 1991
- Identification of a factor in conventional muscle actin preparations which inhibits actin filament self-associationBiochemical and Biophysical Research Communications, 1980