Distinctive tissue distribution and phosphorylation of IRSp53 isoforms.

Abstract	An insulin-receptor substrate of 53-kDa protein (IRSp53) is an adapter protein, which interacts with the Rho-family of GTPases and mediates neurite outgrowth. It also binds to DRPLA protein, a product of the gene responsible for a polyglutamine disease, dentatorubral-pallidoluysian atrophy (DRPLA). Isoforms of human IRSp53 have been reported, each with a unique amino acid sequence at the C-terminal end. Here we report the distinctive tissue distribution and phosphorylation of three isoforms (L, S, and T-forms). Western blotting analyses with isoform-specific antibodies demonstrated that the L and S-forms were expressed in the brain, whereas the T-form was not present in any tissues examined, but was found in a cancer cell line. The L and S-forms were phosphorylated upon stimulation with insulin, and the T-form with IGF-I. Since phospho-acceptor sites were localized to the common portion, the difference in phosphorylation seems to be due to the unique C-terminal sequence.
Authors	Y Okamura-Oho, T Miyashita, M Yamada
Journal	Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 289 Issue 5 Pg. 957-60 (Dec 21 2001) ISSN: 0006-291X [Print] United States
PMID	11741283 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	BAIAP2 protein, human Insulin Nerve Tissue Proteins Protein Isoforms Recombinant Proteins atrophin-1 Tyrosine Insulin-Like Growth Factor I
Topics	Amino Acid Sequence Animals Antibody Specificity Binding Sites Brain (metabolism) Cell Line HeLa Cells Humans Immunochemistry Insulin (pharmacology) Insulin-Like Growth Factor I (pharmacology) Male Molecular Sequence Data Nerve Tissue Proteins (chemistry, genetics, metabolism) Phosphorylation Protein Isoforms (chemistry, genetics, metabolism) Rats Rats, Wistar Recombinant Proteins (chemistry, genetics, metabolism) Tissue Distribution Tyrosine (chemistry)

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