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Cellular interactions of CRKL, and SH2-SH3 adaptor protein

ten Hoeve, J; Kaartinen, V; Fioretos, Thoas LU ; Haataja, L; Voncken, J W; Heisterkamp, N and Groffen, J (1994) In Cancer Research 54(10). p.2563-2567
Abstract
Chronic myelogenous leukemia is characterized by a specific chromosomal translocation, t(9;22), in which the ABL protooncogene and the BCR gene become juxtaposed. The chimeric BCR/ABL gene produces a P210 fusion protein with deregulated tyrosine kinase activity. We have recently isolated a complementary DNA, CRKL, which could code for an adaptor protein consisting of one SH2 and two SH3 domains and lacking any catalytic domain. In the current study, we show that CRKL is highly phosphorylated in the chronic myelogenous leukemia cell line K562 and that it is a substrate for the p210 BCR/ABL and p145 ABL kinases. BCR/ABL and ABL are coimmunoprecipitated with CRKL in vivo, demonstrating that relatively stable complexes are formed. In addition,... (More)
Chronic myelogenous leukemia is characterized by a specific chromosomal translocation, t(9;22), in which the ABL protooncogene and the BCR gene become juxtaposed. The chimeric BCR/ABL gene produces a P210 fusion protein with deregulated tyrosine kinase activity. We have recently isolated a complementary DNA, CRKL, which could code for an adaptor protein consisting of one SH2 and two SH3 domains and lacking any catalytic domain. In the current study, we show that CRKL is highly phosphorylated in the chronic myelogenous leukemia cell line K562 and that it is a substrate for the p210 BCR/ABL and p145 ABL kinases. BCR/ABL and ABL are coimmunoprecipitated with CRKL in vivo, demonstrating that relatively stable complexes are formed. In addition, the nucleotide exchange factor mSOS1 was found to be coimmunoprecipitated with CRKL. These findings establish a putative signal transduction pathway way through which BCR/ABL mediates its oncogenic activity. (Less)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Cancer Research
volume
54
issue
10
pages
2563 - 2567
publisher
American Association for Cancer Research Inc.
external identifiers
  • pmid:8168080
  • scopus:0028301179
ISSN
1538-7445
language
English
LU publication?
no
id
75e25b84-ae57-4386-9092-2327d411dbd5 (old id 1108695)
alternative location
http://cancerres.aacrjournals.org/cgi/reprint/54/10/2563
date added to LUP
2008-07-24 15:06:44
date last changed
2017-08-06 04:23:41
@article{75e25b84-ae57-4386-9092-2327d411dbd5,
  abstract     = {Chronic myelogenous leukemia is characterized by a specific chromosomal translocation, t(9;22), in which the ABL protooncogene and the BCR gene become juxtaposed. The chimeric BCR/ABL gene produces a P210 fusion protein with deregulated tyrosine kinase activity. We have recently isolated a complementary DNA, CRKL, which could code for an adaptor protein consisting of one SH2 and two SH3 domains and lacking any catalytic domain. In the current study, we show that CRKL is highly phosphorylated in the chronic myelogenous leukemia cell line K562 and that it is a substrate for the p210 BCR/ABL and p145 ABL kinases. BCR/ABL and ABL are coimmunoprecipitated with CRKL in vivo, demonstrating that relatively stable complexes are formed. In addition, the nucleotide exchange factor mSOS1 was found to be coimmunoprecipitated with CRKL. These findings establish a putative signal transduction pathway way through which BCR/ABL mediates its oncogenic activity.},
  author       = {ten Hoeve, J and Kaartinen, V and Fioretos, Thoas and Haataja, L and Voncken, J W and Heisterkamp, N and Groffen, J},
  issn         = {1538-7445},
  language     = {eng},
  number       = {10},
  pages        = {2563--2567},
  publisher    = {American Association for Cancer Research Inc.},
  series       = {Cancer Research},
  title        = {Cellular interactions of CRKL, and SH2-SH3 adaptor protein},
  volume       = {54},
  year         = {1994},
}