Distinctive tissue distribution and phosphorylation of IRSp53 isoforms.
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.[1]References
- Distinctive tissue distribution and phosphorylation of IRSp53 isoforms. Okamura-Oho, Y., Miyashita, T., Yamada, M. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
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