Published January 24, 1997
| public
Journal Article
Identification of the Abl- and rasGAP-Associated 62 kDa Protein as a Docking Protein, Dok
- Creators
- Yamanashi, Yuji
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Baltimore, David
Abstract
A 62 kDa protein is highly phosphorylated in many cells containing activated tyrosine kinases. This protein, characterized mainly by its avid association with rasGAP, has proved elusive. Anti-phosphotyrosine antibody was used to purify p62. From peptide sequence, molecular cloning revealed a cDNA encoding a novel protein, p62^(dok), with little homology to others but with a prominent set of tyrosines and nearby sequences suggestive of SH2 binding sites. In cells, v-Abl tyrosine kinase binds and strongly phosphorylates p62^(dok), which then binds rasGAP. A monoclonal antibody, 2C4, to the rasGAP-associated p62 reacts with p62^(dok). Thus, p62^(dok) appears to be the long-sought major substrate of many tyrosine kinases.
Additional Information
© 1997 Cell Press. Under an Elsevier user license. Received 24 October 1996, Revised 25 November 1996. Correspondence should be addressed to D. B. We thank R. Cook for micropeptide sequence and valuable discussions. We also thank N. Carpino, D. Wisniewski, A. Strife, D. Marshak, R. Kobayashi, B. Stillman, and B. Clarkson for sharing their results before publication. We are grateful to P. Svec for nucleotide sequence, C. Roman for 1–2 cells, R. Roth for the 2C4 antibody, G. Cohen and N. Shworak for thoughtful suggestions, B. Chen and K. Alexandropoulos for discussions, and T. Koleske and Z. Songyang for critical reading of this manuscript. Y. Y. was a fellow of the Japan–US Cancer Research Training Program. D. B. is an American Cancer Society Research Professor. This work was supported by National Institutes of Health grant CA-51462 (D. B.).Additional details
- Eprint ID
- 102736
- Resolver ID
- CaltechAUTHORS:20200422-151000172
- Japan–US Cancer Research Training Program
- American Cancer Society
- CA-51462
- NIH
- Created
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2020-04-23Created from EPrint's datestamp field
- Updated
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2021-11-16Created from EPrint's last_modified field