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Akt phosphorylation is essential for nuclear translocation and retention in NGF-stimulated PC12 cells.

Abstract：

:Nerve growth factor (NGF) elicits Akt translocation into the nucleus, where it phosphorylates nuclear targets. Here, we describe that Akt phosphorylation can promote the nuclear translocation of Akt and is necessary for its nuclear retention. Overexpression of Akt-K179A, T308A, S473A-mutant failed to show either nuclear translocation or nuclear Akt phosphorylation, whereas expression of wild-type counterpart elicited profound Akt phosphorylation and induced nuclear translocation under NGF stimulation. Employing the PI3K inhibitor and a variety of mutants PI3K, we showed that nuclear translocation of Akt was mediated by activation of PI3K, and Akt phosphorylation status in the nucleus required PI3K activity. Thus the activity of PI3K might contribute to the nuclear translocation of Akt, and that Akt phosphorylation is essential for its nuclear retention under NGF stimulation conditions.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Xuan Nguyen TL,Choi JW,Lee SB,Ye K,Woo SD,Lee KH,Ahn JY

doi

10.1016/j.bbrc.2006.08.120

subject

Has Abstract

pub_date

2006-10-20 00:00:00

pages

789-98

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)01920-6

journal_volume

349

pub_type

杂志文章

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