The reciprocal role of Egr-1 and Sp family proteins in regulation of the PTP1B promoter in response to the p210 Bcr-Abl oncoprotein-tyrosine kinase

Fukada, T., Tonks, N. K. (July 2001) The reciprocal role of Egr-1 and Sp family proteins in regulation of the PTP1B promoter in response to the p210 Bcr-Abl oncoprotein-tyrosine kinase. Journal of Biological Chemistry, 276 (27). pp. 25512-25519. ISSN 0021-9258

URL: http://www.ncbi.nlm.nih.gov/pubmed/11316810
DOI: 10.1074/jbc.M101354200

Abstract

Protein-tyrosine phosphatase 1B (PTP1B) is an important regulator of protein-tyrosine kinase-dependent signaling pathways. Changes in expression and activity of PTP1B have been associated with various human diseases; however, the mechanisms by which PTP1B expression is regulated have yet to be characterized. Previously, we have shown that the expression of PTP1B is enhanced by p210 Bcr-Ab1 and that PTP1B is a specific antagonist of transformation induced by this oncoprotein protein-tyrosine kinase, Here we have characterized the PTP1B promoter and demonstrate that a motif with features of a stress-response element acts as a (p) under bar 210 Bcr-Ab1-(r) under bar esponsive (s) under bar equence, termed PRS. We have shown that three C2H2 zinc finger proteins, namely Sp1, Sp3, and Egr-1, bind to PRS. Whereas binding of either Spl or Sp3 induced promoter function, Egr-1 repressed Sp3-mediated PTP1B promoter activation. The binding of Egr-1 to PRS is suppressed by p210 Bcr-Ab1 due to the inhibition of Egr-1 expression, resulting in the enhancement of PTP1B promoter activity. Our data indicate that Egr-1 and Sp family proteins play a reciprocal role in the control of expression from the PTP1B promoter.

Item Type: Paper
Uncontrolled Keywords: GATA TRANSCRIPTION FACTORS GROWTH-FACTOR-I SACCHAROMYCES-CEREVISIAE PHOSPHATASE 1B INSULIN SENSITIVITY NEGATIVE REGULATOR SKELETAL-MUSCLE GENE-EXPRESSION BINDING MOTIF ELEMENT STRE
Subjects: diseases & disorders > cancer
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification
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
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > tyrosine kinase
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > protein tyrosine phosphatase
organism description > yeast
CSHL Authors:
Communities: CSHL labs > Tonks lab
Depositing User: Matt Covey
Date: July 2001
Date Deposited: 18 Dec 2013 19:43
Last Modified: 18 Dec 2013 19:43
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29019

Actions (login required)

Administrator's edit/view item Administrator's edit/view item
CSHL HomeAbout CSHLResearchEducationNews & FeaturesCampus & Public EventsCareersGiving