Inhibition of Cell Migration, Spreading, and Focal Adhesions by Tumor Suppressor PTEN

Masahito Tamura; Jianguo Gu; Kazue Matsumoto; Shin‐ichi Aota; Ramon Parsons; Kenneth M. Yamada

doi:10.1126/science.280.5369.1614

Abstract

The tumor suppressor PTEN is a phosphatase with sequence similarity to the cytoskeletal protein tensin. Here the cellular roles of PTEN were investigated. Overexpression of PTEN inhibited cell migration, whereas antisense PTEN enhanced migration. Integrin-mediated cell spreading and the formation of focal adhesions were down-regulated by wild-type PTEN but not by PTEN with an inactive phosphatase domain. PTEN interacted with the focal adhesion kinase FAK and reduced its tyrosine phosphorylation. Overexpression of FAK partially antagonized the effects of PTEN. Thus, PTEN phosphatase may function as a tumor suppressor by negatively regulating cell interactions with the extracellular matrix.

Keywords

PTENTensinFocal adhesionPhosphataseCell migrationCancer researchSuppressorCell biologyExtracellular matrixPTK2Protein tyrosine phosphatasePhosphorylationBiologyChemistryCellSignal transductionPI3K/AKT/mTOR pathwayProtein kinase ACancerBiochemistryGenetics

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Publication Info

Year: 1998
Type: article
Volume: 280
Issue: 5369
Pages: 1614-1617
Citations: 1217
Access: Closed

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APA Style

                            
                                
                                    Masahito Tamura, 
                                
                                    Jianguo Gu, 
                                
                                    Kazue Matsumoto
                                
                                et al.
                            
                            (1998). 
                            Inhibition of Cell Migration, Spreading, and Focal Adhesions by Tumor Suppressor PTEN. 
                            Science
                            , 280
                            (5369)
                            , 1614-1617.
                            https://doi.org/10.1126/science.280.5369.1614
                        

Identifiers

DOI: 10.1126/science.280.5369.1614