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Mammalian target of rapamycin regulates IRS-1 serine 307 phosphorylation.

Abstract：

:Insulin signaling can be negatively regulated by phosphorylation of serine 307 of the insulin receptor substrate (IRS)-1. Rapamycin, an inhibitor of the kinase mTOR, can prevent serine 307 phosphorylation and the development of insulin resistance. We further investigated the role of mTOR in regulating serine 307 phosphorylation, demonstrating that serine 307 phosphorylation in response to insulin, anisomycin, or tumor necrosis factor was quantitatively and temporally associated with activation of mTOR and could be inhibited by rapamycin. Amino acid stimulation activated mTOR and resulted in IRS-1 serine 307 phosphorylation without activating PKB or JNK. Okadaic acid, an inhibitor of the phosphatase PP2A, activated mTOR and stimulated the phosphorylation of serine 307 in a rapamycin-sensitive manner, indicating serine 307 phosphorylation requires mTOR activity but not PP2A, suggesting that mTOR itself may be responsible for phosphorylating serine 307. Finally, we demonstrated that serine 307 phosphorylated IRS-1 is detected primarily in the cytosolic fraction.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Carlson CJ,White MF,Rondinone CM

doi

10.1016/j.bbrc.2004.02.082

subject

Has Abstract

pub_date

2004-04-02 00:00:00

pages

533-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006291X04003407

journal_volume

316

pub_type

杂志文章

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