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

20 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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10.1074/jbc.M113.527564

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@article{b417a46dd85b4af1b9b71fc120d675f4,

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",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology Inc.",

number = "52",

}

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.

UR - https://www.scopus.com/pages/publications/84891397565

UR - https://www.scopus.com/pages/publications/84891397565#tab=citedBy

U2 - 10.1074/jbc.M113.527564

DO - 10.1074/jbc.M113.527564

M3 - Article

C2 - 24217252

AN - SCOPUS:84891397565

SN - 0021-9258

VL - 288

SP - 36926

EP - 36935

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 52

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

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