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)
- Institution
- 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.
Polyphosphoinositides inhibit the interaction of vinculin with actin filaments
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Created on 1/1/1999
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Additional Information
- Publication
- Journal of Biological Chemistry. 274:18414-18420
- Language: English
- Date: 1999
- Keywords
- vinculin, actin filaments, polyphosphoinositides, talin