p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells

Carpino, N., Wisniewski, D., Strife, A., Marshak, D., Kobayashi, R., Stillman, B., Clarkson, B. (January 1997) p62(dok): a constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells. Cell, 88 (2). pp. 197-204. ISSN 0092-8674 (Print)

Abstract

Characteristic of chronic myelogenous leukemia (CML) is the presence of the chimeric p210(bcr-abl) protein possessing elevated protein tyrosine kinase activity relative to normal c-abl tyrosine kinase. Hematopoietic progenitors isolated from CML patients in the chronic phase contain a constitutively tyrosine-phosphorylated protein that migrates at 62 kDa by SDS-PAGE and associates with the p120 ras GTPase-activating protein (GAP). We have purified p62(dok) from a hematopoietic cell line expressing p210(bcr-abl). p62(dok) is a novel protein with features of a signaling molecule. Association of p62(dok) with GAP correlates with its tyrosine phosphorylation. p62(dok) is rapidly tyrosine-phosphorylated upon activation of the c-Kit receptor, implicating it as a component of a signal transduction pathway downstream of receptor tyrosine kinases.

Item Type: Paper
Uncontrolled Keywords: Cloning, Molecular DNA-Binding Proteins Electrophoresis Polyacrylamide Gel Fusion Proteins bcr-abl metabolism GTPase-Activating Proteins Hematopoietic Stem Cells metabolism Humans Leukemia, Myeloid, Chronic metabolism Phosphoproteins chemistry isolation & purification metabolism Phosphorylation Phosphotyrosine metabolism Protein-Tyrosine Kinase metabolism Proteins metabolism Proto-Oncogene Proteins c-kit metabolism RNA-Binding Proteins Signal Transduction Stem Cell Factor metabolism Tumor Cells, Cultured ras GTPase-Activating Proteins src Homology Domains
Subjects: diseases & disorders > cancer > cancer types > leukemia
biotechnology > chromatography > protein purification
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes > kinase > tyrosine kinase
CSHL Authors:
Communities: CSHL labs > Kobayashi lab
CSHL labs > Stillman lab
Highlight: Stillman, Bruce W.
Depositing User: CSHL Librarian
Date: 24 January 1997
Date Deposited: 07 Mar 2012 18:36
Last Modified: 20 Jun 2017 19:35
Related URLs:
URI: https://repository.cshl.edu/id/eprint/24946

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