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Type Iγ phosphatidylinositol phosphate kinase targets and regulates focal adhesions

Type Iγ phosphatidylinositol phosphate kinase targets and regulates focal adhesions The ability of cells to form cell contacts, adhere to the extracellular matrix, change morphology, and migrate is essential for development, wound healing, metastasis, cell survival and the immune response. These events depend on the binding of integrin to the extracellular matrix, and assembly of focal adhesions, which are complexes comprising scaffolding and signalling proteins organized by adhesion to the extracellular matrix 1,2,3 . Phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) regulates interactions between these proteins, including the interaction of vinculin with actin and talin 4,5,6,7,8,9 . The binding of talin to β-integrin is strengthened by PtdIns(4,5)P2, suggesting that the basis of focal adhesion assembly is regulated by this lipid mediator 9,10 . Here we show that the type I phosphatidylinositol phosphate kinase isoform-γ 661 (PIPKIγ661), an enzyme that makes PtdIns(4,5)P2, is targeted to focal adhesions by an association with talin. PIPKIγ661 is tyrosine phosphorylated by focal adhesion associated kinase signalling, increasing both the activity of phosphatidylinositol phosphate kinase and its association with talin. This defines a mechanism for spatial generation of PtdIns(4,5)P2 at focal adhesions. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Springer Journals

Type Iγ phosphatidylinositol phosphate kinase targets and regulates focal adhesions

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References (32)

Publisher
Springer Journals
Copyright
Copyright © 2002 by Macmillan Magazines Ltd.
Subject
Science, Humanities and Social Sciences, multidisciplinary; Science, Humanities and Social Sciences, multidisciplinary; Science, multidisciplinary
ISSN
0028-0836
eISSN
1476-4687
DOI
10.1038/nature01082
Publisher site
See Article on Publisher Site

Abstract

The ability of cells to form cell contacts, adhere to the extracellular matrix, change morphology, and migrate is essential for development, wound healing, metastasis, cell survival and the immune response. These events depend on the binding of integrin to the extracellular matrix, and assembly of focal adhesions, which are complexes comprising scaffolding and signalling proteins organized by adhesion to the extracellular matrix 1,2,3 . Phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) regulates interactions between these proteins, including the interaction of vinculin with actin and talin 4,5,6,7,8,9 . The binding of talin to β-integrin is strengthened by PtdIns(4,5)P2, suggesting that the basis of focal adhesion assembly is regulated by this lipid mediator 9,10 . Here we show that the type I phosphatidylinositol phosphate kinase isoform-γ 661 (PIPKIγ661), an enzyme that makes PtdIns(4,5)P2, is targeted to focal adhesions by an association with talin. PIPKIγ661 is tyrosine phosphorylated by focal adhesion associated kinase signalling, increasing both the activity of phosphatidylinositol phosphate kinase and its association with talin. This defines a mechanism for spatial generation of PtdIns(4,5)P2 at focal adhesions.

Journal

Nature – Springer Journals

Published: Nov 7, 2002

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