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

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

Research output: Contribution to journal › Article › peer-review

1110 Scopus citations

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.

Original language	English
Pages (from-to)	1614-1617
Number of pages	4
Journal	Science
Volume	280
Issue number	5369
DOIs	https://doi.org/10.1126/science.280.5369.1614
State	Published - 5 Jun 1998
Externally published	Yes

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title = "Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN",

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.",

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T1 - Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN

AU - Tamura, Masahito

AU - Gu, Jianguo

AU - Matsumoto, Kazue

AU - Aota, Shin Ichi

AU - Parsons, Ramon

AU - Yamada, Kenneth M.

PY - 1998/6/5

Y1 - 1998/6/5

N2 - 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.

AB - 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.

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VL - 280

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EP - 1617

JO - Science

JF - Science

IS - 5369

ER -

Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN

Abstract

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