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Regulation of ezrin localization by Rac1 and PIPK in human epithelial cells
- Source :
- Experimental Cell Research. 313:824-833
- Publication Year :
- 2007
- Publisher :
- Elsevier BV, 2007.
-
Abstract
- Regulation of ezrin and other ERM proteins is not completely understood, but the involvement of Rho GTPases seems crucial. In this work, expression plasmids encoding full-length, deleted or truncated ezrin were constructed and coexpressed with Rac1 GTPase in HeLa human epithelial cells in order to elucidate the mechanisms of ezrin activation and function. We observed induction of actin stress fiber formation by ezrin constructs harboring the F-actin binding site but devoid of sequences required for intra- or intermolecular binding. Stress fiber-inducing ezrin mutants were localized in adherens junctions containing N-cadherin but no E-cadherin, and also colocalized with F-actin in stress fibers. This localization required the activity of Rac1 and phosphatidylinositol-4-phosphate 5-kinase and involved RhoA. We suggest that localization of ezrin in adherens junctions is regulated by Rac in a manner involving PIPK.
- Subjects :
- rac1 GTP-Binding Protein
Stress fiber
RHOA
RAC1
macromolecular substances
Biology
Transfection
environment and public health
Adherens junction
Ezrin
Humans
Tissue Distribution
Cloning, Molecular
Actin
Cadherin
Epithelial Cells
Adherens Junctions
Cell Biology
Cell biology
Cytoskeletal Proteins
Phosphotransferases (Alcohol Group Acceptor)
biology.protein
rhoA GTP-Binding Protein
Gene Deletion
HeLa Cells
Subjects
Details
- ISSN :
- 00144827
- Volume :
- 313
- Database :
- OpenAIRE
- Journal :
- Experimental Cell Research
- Accession number :
- edsair.doi.dedup.....cd318224ff5322215629f5eb9418170d