Akt2 phosphorylates Synip to regulate docking and fusion of GLUT4-containing vesicles

We have identified an unusual potential dual Akt/protein kinase B consensus phosphorylation motif in the protein Synip (RxKxRS(97)xS(99)). Surprisingly, serine 97 is not appreciably phosphorylated, whereas serine 99 is only a specific substrate for Akt2 but not Akt1 or Akt3. Although wild-type Synip...

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Hlavní autoři: Yamada, Eijiro, Okada, Shuichi, Saito, Tsugumichi, Ohshima, Kihachi, Sato, Minoru, Tsuchiya, Takafumi, Uehara, Yutaka, Shimizu, Hiroyuki, Mori, Masatomo
Médium: Artigo
Jazyk:Inglês
Vydáno: The Rockefeller University Press 2005
Témata:
Research Articles
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2171785/
https://ncbi.nlm.nih.gov/pubmed/15753124
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1083/jcb.200408182
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