C-src Activates Endonuclease-mediated Mrna Decay.
From: Department of Molecular and Cellular Biochemistry, The RNA Group and the Comprehensive Cancer Center, The Ohio State University, Columbus, OH 43210, USA.
Molecular cell
- Publish Date: Mar 2007
- ISSN: 1097-2765
- Volume: 25
- Issue: 5
- Pages: 779-87
- Medium: Print
- Language: English
- Citation (JAMA): Peng Yong, Schoenberg Daniel R, et al. C-src Activates Endonuclease-mediated Mrna Decay.. Mol. Cell Mar 2007;25:779-87
Abstract
The mRNA endonuclease PMR1 initiates mRNA decay by forming a selective complex with its translating substrate mRNA. Previous work showed that the ability of PMR1 to target to polysomes and activate decay depends on the phosphorylation of a tyrosine residue at position 650. The current study shows that c-Src is responsible for activating this mRNA decay pathway. c-Src was recovered with immunoprecipitated PMR1, and it phosphorylates PMR1 in vitro and in vivo. The interaction with c-Src involves two domains of PMR1: Y650 and a series of proline-rich SH3 peptides in the N terminus. In cells with little c-Src, PMR1 targeting to polysomes is induced by constitutively active c-Src but not by inactive forms of the kinase. Similarly, only active c-Src induces PMR1-mediated mRNA decay. Finally, we show that EGF rapidly induces c-Src phosphorylation of PMR1, providing a direct link between tyrosine kinase-mediated signal transduction and mRNA decay.
Mesh Headings (Keywords): Animals, Binding Sites, COS Cells, Catalysis, Cercopithecus aethiops, Endonucleases, Endoribonucleases, Enzyme Activation, Mutant Proteins, Phosphorylation, Phosphotyrosine, Polyribosomes, Protein Binding, Proto-Oncogene Proteins pp60(c-src), RNA Stability, RNA, Messenger, Xenopus, Xenopus Proteins, src Homology Domains
Check for Full Text / PubMed Unique Identifier (PMID): 17349962
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