Polyphosphoinositides inhibit the interaction of vinculin with actin filaments

UNCG Author/Contributor (non-UNCG co-authors, if there are any, appear on document)
Paul A. Steimle, Assistant Professor (Creator)
The University of North Carolina at Greensboro (UNCG )
Web Site: http://library.uncg.edu/

Abstract: Binding of vinculin to adhesion plaque proteins is restricted by an intramolecular association of vinculin’s head and tail regions. Results of previous work suggest that polyphosphoinositides disrupt this interaction and thereby promote binding of vinculin to both talin and actin. However, data presented here show that phosphatidylinositol 4,5-bisphosphate (PI4,5P2) inhibits the interaction of purified tail domain with F-actin.

Additional Information

Journal of Biological Chemistry. 274:18414-18420
Language: English
Date: 1999
vinculin, actin filaments, polyphosphoinositides, talin

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