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 Lettjournal_title
FEBS lettersauthors
Murray JT,Cummings LA,Bloomberg GB,Cohen Pdoi
10.1016/j.febslet.2004.12.069keywords:
subject
Has Abstractpub_date
2005-02-14 00:00:00pages
991-4issue
5eissn
0014-5793issn
1873-3468pii
S0014-5793(05)00027-Xjournal_volume
579pub_type
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