| Involvement of PRMT1 in hnRNPQ activation and internalization of insulin receptor. | |
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MedLine Citation:
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PMID: 18492485 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Insulin signaling in skeletal L6 myotubes is known to be affected by arginine methylation catalyzed by protein N-arginine methyltransferase 1 (PRMT1), however, the mechanism by which this occurs has not yet been defined. This study aimed to determine the exact substrate involved in the methylation and regulating insulin signaling in cells. Insulin enhanced arginine methylation of a 66-kDa protein (p66) concomitant with translocation of PRMT1 to the membrane fraction. Peptide mass fingerprinting identified p66 as a heterogeneous nuclear ribonucleoprotein, hnRNPQ that was bound to and methylated by PRMT1. Pharmacological inhibition of methylation (MTA) and small interfering RNA against PRMT1 (PRMT1-siRNA) attenuated insulin-stimulated tyrosine phosphorylation of hnRNPQ and insulin receptor (IR), and the interaction between hnRNPQ and IR. MTA, PRMT1-siRNA, and hnRNPQ-siRNA inhibited internalization of IR in the same manner. These data suggest that the PRMT1-mediated methylation of hnRNPQ is implicated in IR trafficking and insulin signaling in skeletal L6 myotubes. |
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Authors:
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Hiroaki Iwasaki |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-05-19 |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: 372 ISSN: 1090-2104 ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2008 Jul |
Date Detail:
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Created Date: 2008-06-10 Completed Date: 2008-08-12 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: United States |
Other Details:
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Languages: eng Pagination: 314-9 Citation Subset: IM |
Affiliation:
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Division of Endocrinology and Metabolism, Department of Internal Medicine, Toshiba Rinkan Hospital, 7-9-1 Kami-tsuruma, Sagamihara, Kanagawa 228-8585, Japan. hiwasaki-dm@umin.net |
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Arginine / metabolism Heterogeneous-Nuclear Ribonucleoproteins / genetics, metabolism* Humans Insulin / metabolism*, pharmacology Methylation / drug effects Molecular Sequence Data Myoblasts / metabolism Phosphorylation / drug effects Protein-Arginine N-Methyltransferases / genetics, metabolism* RNA, Small Interfering / genetics Rats Receptor, Insulin / metabolism* Tyrosine / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Heterogeneous-Nuclear Ribonucleoproteins; 0/RNA, Small Interfering; 0/hnRNPQ protein, rat; 11061-68-0/Insulin; 55520-40-6/Tyrosine; 74-79-3/Arginine; EC 2.1.1.-/Protein-Arginine N-Methyltransferases; EC 2.7.10.1/Receptor, Insulin |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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