Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoproteinmediated mammary epithelial cell motility

Benoit Boivin; Fauzia Chaudhary; Bryan C. Dickinson; Aftabul Haque; Stephanie C. Pero; Christopher J. Chang; Nicholas K. Tonks

doi:10.1074/jbc.M113.527564

Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoproteinmediated mammary epithelial cell motility

Benoit Boivin, Fauzia Chaudhary, Bryan C. Dickinson, Aftabul Haque, Stephanie C. Pero, Christopher J. Chang, Nicholas K. Tonks

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

19 Scopus citations

Abstract

Background: PTPα has been implicated in breast cancer, but its function remains to be defined. Results: Suppression of PTPα led to a GRB7-dependent, ErbB2-mediated increase in mammary epithelial cell migration. PTPα dephosphorylated FAK on Tyr-407. Conclusion: PTPα functions to suppress ErbB2 signaling events that lead to migration of breast cancer cells. Significance: PTPα may play positive or negative roles in signaling, depending upon context.

Original language	English (US)
Pages (from-to)	36926-36935
Number of pages	10
Journal	Journal of Biological Chemistry
Volume	288
Issue number	52
DOIs	https://doi.org/10.1074/jbc.M113.527564
State	Published - Dec 27 2013
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology
Cell Biology

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title = "Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoproteinmediated mammary epithelial cell motility",

abstract = "Background: PTPα has been implicated in breast cancer, but its function remains to be defined. Results: Suppression of PTPα led to a GRB7-dependent, ErbB2-mediated increase in mammary epithelial cell migration. PTPα dephosphorylated FAK on Tyr-407. Conclusion: PTPα functions to suppress ErbB2 signaling events that lead to migration of breast cancer cells. Significance: PTPα may play positive or negative roles in signaling, depending upon context.",

author = "Benoit Boivin and Fauzia Chaudhary and Dickinson, {Bryan C.} and Aftabul Haque and Pero, {Stephanie C.} and Chang, {Christopher J.} and Tonks, {Nicholas K.}",

year = "2013",

month = dec,

day = "27",

doi = "10.1074/jbc.M113.527564",

language = "English (US)",

volume = "288",

pages = "36926--36935",

journal = "Journal of Biological Chemistry",

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TY - JOUR

T1 - Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoproteinmediated mammary epithelial cell motility

AU - Boivin, Benoit

AU - Chaudhary, Fauzia

AU - Dickinson, Bryan C.

AU - Haque, Aftabul

AU - Pero, Stephanie C.

AU - Chang, Christopher J.

AU - Tonks, Nicholas K.

PY - 2013/12/27

Y1 - 2013/12/27

N2 - Background: PTPα has been implicated in breast cancer, but its function remains to be defined. Results: Suppression of PTPα led to a GRB7-dependent, ErbB2-mediated increase in mammary epithelial cell migration. PTPα dephosphorylated FAK on Tyr-407. Conclusion: PTPα functions to suppress ErbB2 signaling events that lead to migration of breast cancer cells. Significance: PTPα may play positive or negative roles in signaling, depending upon context.

AB - Background: PTPα has been implicated in breast cancer, but its function remains to be defined. Results: Suppression of PTPα led to a GRB7-dependent, ErbB2-mediated increase in mammary epithelial cell migration. PTPα dephosphorylated FAK on Tyr-407. Conclusion: PTPα functions to suppress ErbB2 signaling events that lead to migration of breast cancer cells. Significance: PTPα may play positive or negative roles in signaling, depending upon context.

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JF - Journal of Biological Chemistry

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ER -

Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoproteinmediated mammary epithelial cell motility

Abstract

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