NDLI: Tensin1 Requires Protein Phosphatase-1α in Addition to RhoGAP DLC-1 to Control Cell Polarization, Migration, and Invasion

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Tensin1 Requires Protein Phosphatase-1α in Addition to RhoGAP DLC-1 to Control Cell Polarization, Migration, and Invasion

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Tensin1 Requires Protein Phosphatase-1α in Addition to RhoGAP DLC-1 to Control Cell Polarization, Migration, and Invasion

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Daugherty, Abbi E. Hall, Emily H. Brautigan, David L. Horwitz, Alan F. Choi, Colin K.
Description	Author Affiliation: Hall EH ( Center for Cell Signaling and Department of Microbiology, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA.)
Abstract	Tensin is a family of multidomain scaffold proteins that bind the cytoplasmic tail of beta-integrins and localize to adhesions that anchor stress fibers in cells. Tensin expression is suppressed in cancer, especially metastatic cancer. The N-terminal domain of tensin1 associates with protein phosphatase-1alpha (PP1alpha) and mediates PP1alpha localization to adhesions. Here, we show F302A mutation in a KVXF motif of tensin1 abrogates binding to PP1alpha. The SH2 domain in tensin family member c-ten requires R474 to bind a RhoGAP called DLC-1 (deleted in liver cancer). We mutated the corresponding residue in tensin1, R1488A, and showed this reduces association with DLC-1. Unexpectedly, tensin1 F302A also had reduced association with DLC-1. Expression of tensin1 F302A or R1488A showed similar dominant phenotypes, with reduced cell polarization, lowered MLC20 phosphorylation and reduced levels of RhoA(GTP) compared with cells expressing tensin1 WT. However, migration and invasion of metastatic MDA MB 231 breast cancer cells were differentially affected by tensin1 mutated at F302A or R1488A. Cancer cells stably expressing F302A tensin1 showed increased migration and invasion compared with cells stably expressing either R1488A tensin1 or WT tensin1. This suggests that PP1alpha bound to tensin1 has additional effects in reducing migration and invasion that are not mediated through DLC-1. Our results show the importance of PP1alpha binding to tensin1 for the regulation of cell polarization, migration, and invasion.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	50
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-12-11
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cell Movement Physiology Cell Polarity Microfilament Proteins Metabolism Protein Phosphatase 1 Tumor Suppressor Proteins Amino Acid Sequence Animals Cell Adhesion Cell Line Cell Shape Enzyme Activation GTPase-Activating Proteins Genetics Molecular Sequence Data Neoplasm Invasiveness Physiopathology Neoplasms Pathology Point Mutation Recombinant Fusion Proteins RhoA GTP-Binding Protein Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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