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

  


Authors: Carpino, N.; Wisniewski, D.; Strife, A.; Marshak, D.; Kobayashi, R.; Stillman, B.; Clarkson, B.
Article Title: p62(dok): A constitutively tyrosine-phosphorylated, GAP-associated protein in chronic myelogenous leukemia progenitor cells
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.
Keywords: signal transduction; protein phosphorylation; human cell; dna-binding proteins; proteins; stem cell factor; proto-oncogene proteins c-kit; protein protein interaction; cell differentiation; tumor cells, cultured; enzyme activity; chronic myeloid leukemia; tyrosine; phosphorylation; cloning, molecular; rna-binding proteins; protein processing; protein transport; growth regulation; hematopoietic stem cells; phosphoproteins; guanosine triphosphatase activating protein; gtpase-activating proteins; ras protein; protein-tyrosine kinases; hematopoietic stem cell; fusion proteins, bcr-abl; electrophoresis, polyacrylamide gel; phosphotyrosine; leukemia, myeloid, chronic; humans; human; priority journal; article; src homology domains; ras gtpase-activating proteins
Journal Title: Cell
Volume: 88
Issue: 2
ISSN: 0092-8674
Publisher: Cell Press  
Date Published: 1997-01-24
Start Page: 197
End Page: 204
Language: English
DOI: 10.1016/s0092-8674(00)81840-1
PUBMED: 9008160
PROVIDER: scopus
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0031459864&doi=10.1016%2fS0092-8674%2800%2981840-1&partnerID=40&md5=57e222fdffa9c3e303d47bc229f699b3
Notes: Article -- Export Date: 17 March 2017 -- Source: Scopus
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MSK Authors
  1. David Wisniewski
    37 Wisniewski
  2. Bayard Clarkson
    220 Clarkson
  3. Annabel Strife
    41 Strife
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