Identification of different specificity requirements between SGK1 and PKBalpha.

Abstract:

:NDRG1 is phosphorylated by SGK1 (but not PKB) in vivo at three residues each contained within three nonapeptide repeats. Here, we demonstrate that this nonapeptide, like the NDRG1 protein, is phosphorylated by SGK1, but not by PKBalpha or RSK1 in vitro. The inability of PKBalpha and RSK1 to phosphorylate the nonapeptide was traced to residues n+1, n+2 and n-4 (where n is the phosphorylation site). Changing them from Ser, Glu and Ser to Phe, Ala and Pro, respectively, transformed the nonapeptide into an excellent substrate for PKBalpha and RSK1. Our results identify a specific substrate for SGK1 and may facilitate detection of additional physiological substrates for this enzyme.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Murray JT,Cummings LA,Bloomberg GB,Cohen P

doi

10.1016/j.febslet.2004.12.069

keywords:

subject

Has Abstract

pub_date

2005-02-14 00:00:00

pages

991-4

issue

5

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(05)00027-X

journal_volume

579

pub_type

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