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p62 : A Constitutively Tyrosine-Phosphorylated, GAP-Associated Protein in Chronic Myelogenous Leukemia Progenitor Cells
Open accessAbstract
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.
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Protein modules and signalling networks
Pawson, T. (1995) · Nature · doi:10.1038/373573a0 · Cited by 2,420
A Cytoplasmic Protein Stimulates Normal N- ras p21 GTPase, But Does Not Affect Oncogenic Mutants
Trahey, M., & McCormick, F. (1987) · Science · doi:10.1126/science.2821624 · Cited by 1,211
Modular binding domains in signal transduction proteins
Cohen, G. B., Ren, R., & Baltimore, D. (1995) · Cell · doi:10.1016/0092-8674(95)90406-9 · Cited by 951
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(1998) · PubMed · Cited by 2,737
Sawyers, C. L. (1999) · New England Journal of Medicine · doi:10.1056/nejm199904293401706 · Cited by 1,621
The IL-4 receptor: signaling mechanisms and biologic functions
Nelms, K., Keegan, A. D., Zamorano, J., Ryan, J. J., & Paul, W. E. (1999) · Annual Review of Immunology · doi:10.1146/annurev.immunol.17.1.701 · Cited by 1,545
Protein–protein interaction in insulin signaling and the molecular mechanisms of insulin resistance
Virkamäki, A., Ueki, K., & Kahn, C. R. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6609 · Cited by 854
The IRS-signalling system: A network of docking proteins that mediate insulin action
White, M. F. (1998) · Insulin Action · doi:10.1007/978-1-4615-5647-3_1 · Cited by 667
Metadata
- Authors
- Carpino, N., Wisniewski, D., Strife, A., Marshak, D., Kobayashi, R., Stillman, B., & Clarkson, B.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-01
- Volume
- 88
- Issue
- 2
- Pages
- 197-204
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2093670935
- Cited by
- 362
- References
- 3
- FWCI
- 25.74
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: p62 : A Constitutively Tyrosine-Phosphorylated, GAP-Associated Protein in Chronic Myelogenous Leukemia Progenitor Cells. https://app.cochat.ai/papers/10.1016/s0092-8674(00)81840-1
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- Carpino, N., Wisniewski, D., Strife, A., Marshak, D., Kobayashi, R., Stillman, B., & Clarkson, B. (1997). p62 : A Constitutively Tyrosine-Phosphorylated, GAP-Associated Protein in Chronic Myelogenous Leukemia Progenitor Cells. Cell. https://doi.org/10.1016/s0092-8674(00)81840-1
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
