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

Boivin, B., Chaudhary, F., Dickinson, B. C., Haque, A., Pero, S. C., Chang, C. J., Tonks, N. K. (November 2013) Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoprotein mediated mammary epithelial cell motility. Journal of Biological Chemistry, 288 (52). pp. 36926-36935. ISSN 00219258 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/24217252
DOI: 10.1074/jbc.M113.527564

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.

Item Type: Paper
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > ErbB
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
diseases & disorders > cancer > cancer types > breast cancer
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > genes, structure and function > genes: types > oncogene
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
CSHL Authors:
Communities: CSHL labs > Tonks lab
CSHL Cancer Center Program > Signal Transduction
Depositing User: Matt Covey
Date: November 2013
Date Deposited: 22 Jan 2014 22:06
Last Modified: 15 Oct 2015 16:34
PMCID: PMC3873551
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29338

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