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Biochemical characterization of rolledSem, an activated form of Drosophila mitogen-activated protein kinase.


Oellers, N; Hafen, E (1996). Biochemical characterization of rolledSem, an activated form of Drosophila mitogen-activated protein kinase. Journal of Biological Chemistry, 271(40):24939-24944.

Abstract

The rolled (rl) gene of Drosophila encodes a homologue of vertebrate mitogen-activated protein kinases. Genetic analyses have shown that the gain-of-function mutation rolledSevenmaker (rlSem) is sufficient to activate developmental pathways controlled by distinct receptor tyrosine kinases, such as Sevenless, Torso, and the Drosophila epidermal growth factor receptor homologue. Here we show that mutant RlSem protein, immunoprecipitated from transiently transfected COS cells, exhibits a moderate increase in kinase activity compared with wild-type Rl protein. Time course studies revealed that RlSem is more active than Rl following short term as well as prolonged treatment with epidermal growth factor. Interestingly, a more pronounced difference in kinase activity is observed when the proteins are immunoprecipitated from extracts of Drosophila rl and rlSem larvae. In fact, the kinase activity of RlSem from larvae extracts is comparable to the kinase activity of larvae expressing either an activated Sevenless receptor or an activated Raf kinase. We also demonstrate that Dsor1, which has been placed upstream of rl genetically, is able to phosphorylate and activate Rl in vitro.

The rolled (rl) gene of Drosophila encodes a homologue of vertebrate mitogen-activated protein kinases. Genetic analyses have shown that the gain-of-function mutation rolledSevenmaker (rlSem) is sufficient to activate developmental pathways controlled by distinct receptor tyrosine kinases, such as Sevenless, Torso, and the Drosophila epidermal growth factor receptor homologue. Here we show that mutant RlSem protein, immunoprecipitated from transiently transfected COS cells, exhibits a moderate increase in kinase activity compared with wild-type Rl protein. Time course studies revealed that RlSem is more active than Rl following short term as well as prolonged treatment with epidermal growth factor. Interestingly, a more pronounced difference in kinase activity is observed when the proteins are immunoprecipitated from extracts of Drosophila rl and rlSem larvae. In fact, the kinase activity of RlSem from larvae extracts is comparable to the kinase activity of larvae expressing either an activated Sevenless receptor or an activated Raf kinase. We also demonstrate that Dsor1, which has been placed upstream of rl genetically, is able to phosphorylate and activate Rl in vitro.

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Additional indexing

Item Type:Journal Article, refereed
Communities & Collections:07 Faculty of Science > Institute of Zoology (former)
Dewey Decimal Classification:570 Life sciences; biology
590 Animals (Zoology)
Language:English
Date:4 October 1996
Deposited On:11 Feb 2008 12:16
Last Modified:26 Aug 2016 07:32
Publisher:American Society for Biochemistry and Molecular Biology
ISSN:0021-9258
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:10.1074/jbc.271.40.24939
Related URLs:http://www.jbc.org/cgi/content/abstract/271/40/24939
PubMed ID:8798773
Permanent URL: http://doi.org/10.5167/uzh-618

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