P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase

Myers, M. P., Stolarov, J. P., Eng, C., Li, J., Wang, S. I., Wigler, M. H., Parsons, R., Tonks, N. K. (August 1997) P-TEN, the tumor suppressor from human chromosome 10q23, is a dual-specificity phosphatase. Proc Natl Acad Sci U S A, 94 (17). pp. 9052-7. ISSN 0027-8424 (Print)

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URL: https://www.ncbi.nlm.nih.gov/pubmed/9256433

Abstract

Protein tyrosine phosphatases (PTPs) have long been thought to play a role in tumor suppression due to their ability to antagonize the growth promoting protein tyrosine kinases. Recently, a candidate tumor suppressor from 10q23, termed P-TEN, was isolated, and sequence homology was demonstrated with members of the PTP family, as well as the cytoskeletal protein tensin. Here we show that recombinant P-TEN dephosphorylated protein and peptide substrates phosphorylated on serine, threonine, and tyrosine residues, indicating that P-TEN is a dual-specificity phosphatase. In addition, P-TEN exhibited a high degree of substrate specificity, showing selectivity for extremely acidic substrates in vitro. Furthermore, we demonstrate that mutations in P-TEN, identified from primary tumors, tumor cells lines, and a patient with Bannayan-Zonana syndrome, resulted in the ablation of phosphatase activity, demonstrating that enzymatic activity of P-TEN is necessary for its ability to function as a tumor suppressor.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Chromosomes Human Pair 10 Enzyme Activation Genes Tumor Suppressor Humans Molecular Sequence Data Mutation PTEN Phosphohydrolase Phosphoprotein Phosphatase genetics metabolism Phosphorylation Protein Tyrosine Phosphatase genetics metabolism Substrate Specificity
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > PTEN
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 > DNA, RNA structure, function, modification > suppressor
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 labs > Wigler lab
Depositing User: CSHL Librarian
Date: 19 August 1997
Date Deposited: 11 Apr 2012 20:12
Last Modified: 09 Nov 2017 17:23
PMCID: PMC23024
Related URLs:
URI: http://repository.cshl.edu/id/eprint/26235

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