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Article

Synip phosphorylation is required for insulin-stimulated Glut4 translocation.

Biochemical and biophysical research communications - 27 Apr 2007

Okada Shuichi, Ohshima Kihachi, Uehara Yutaka, Shimizu Hiroyuki, Hashimoto Koshi, Yamada Masanobu, Mori Masatomo

Abstract excerpt

Previously we identified an unusual potential dual Akt/protein kinase B consensus phosphorylation motif in the protein Synip (RxKxRS(97)xS(99)) with serine 99 as a unique Akt2, but not Akt1 or for Akt3, substrate phosphorylation site. Although we have previously reported that serine 99 to phenylalanine (S99F-Synip) resulted in a constitutive inhibition of insulin-stimulated Glut4 translocation, a recent report...

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Identifiers

PMID: 17336927
DOI: 10.1016/j.bbrc.2007.02.095

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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