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

Nick Carpino, David Wisniewski, Annabel Strife, Daniel Marshak, Ryuji Kobayashi, Bruce Stillman, Bayard Clarkson

Research output: Contribution to journalArticlepeer-review

351 Scopus citations

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.

Original languageEnglish
Pages (from-to)197-204
Number of pages8
JournalCell
Volume88
Issue number2
DOIs
StatePublished - 24 Jan 1997
Externally publishedYes

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