NDLI: Tyrosine phosphorylation of p62dok by p210bcr-abl inhibits RasGAP activity

Content Provider	PubMed Central
Author	Kashige, Nobuhiro Carpino, Nick Kobayashi, Ryuji
Copyright Year	2000
Abstract	The t(9;22) chromosomal translocation is found in almost all patients with chronic myelogenous leukemia. The resultant Bcr-Abl fusion gene expresses a chimeric fusion protein p210bcr-abl with increased tyrosine kinase activity. Hematopoietic progenitors isolated from chronic myelogenous leukemia patients in the chronic phase contain constitutively tyrosine-phosphorylated p62dok protein. p62dok associates with the Ras GTPase-activating protein (RasGAP), but only when p62dok is tyrosine phosphorylated. Here we have investigated the interaction between p62dok and RasGAP and the consequences of p62dok tyrosine phosphorylation on the activity of RasGAP. We have found that p62dok is directly tyrosine phosphorylated by p210bcr-abl, and the sites of phosphorylation are located in the C-terminal half of the p62dok molecule. We have identified five tyrosine residues that are involved in in vitro RasGAP binding and have found that tyrosine-phosphorylated p62dok inhibits RasGAP activity. Our results suggest that p210bcr-abl might lead to the activation of the Ras signaling pathway by inhibiting a key down-regulator of Ras signaling.
Related Links	http://dx.doi.org/10.1073/pnas.040547997
Ending Page	2098
Page Count	6
Starting Page	2093
File Format	PDF
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	5
Volume Number	97
Language	English
Publisher	The National Academy of Sciences
Publisher Date	2000-02-29
Access Restriction	Open
Rights Holder	The National Academy of Sciences
Subject Keyword	General Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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