Identification of different specificity requirements between SGK1 and PKBα

James T. Murray; Lorna A. Cummings; Graham B. Bloomberg; Philip Cohen

doi:10.1016/j.febslet.2004.12.069

Identification of different specificity requirements between SGK1 and PKBα

James T. Murray (Lead / Corresponding author), Lorna A. Cummings, Graham B. Bloomberg, Philip Cohen

Research output: Contribution to journal › Article › peer-review

41 Citations (Scopus)

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 PKBα or RSK1 in vitro. The inability of PKBα 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 PKBα and RSK1. Our results identify a specific substrate for SGK1 and may facilitate detection of additional physiological substrates for this enzyme.

Original language	English
Pages (from-to)	991-994
Number of pages	4
Journal	FEBS Letters
Volume	579
Issue number	5
DOIs	https://doi.org/10.1016/j.febslet.2004.12.069
Publication status	Published - 14 Feb 2005

Keywords

NDRG1
PKB
Protein kinase specificity
SGK

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "Identification of different specificity requirements between SGK1 and PKBα",

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 PKBα or RSK1 in vitro. The inability of PKBα 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 PKBα and RSK1. Our results identify a specific substrate for SGK1 and may facilitate detection of additional physiological substrates for this enzyme.",

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T1 - Identification of different specificity requirements between SGK1 and PKBα

AU - Murray, James T.

AU - Cummings, Lorna A.

AU - Bloomberg, Graham B.

AU - Cohen, Philip

PY - 2005/2/14

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N2 - 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 PKBα or RSK1 in vitro. The inability of PKBα 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 PKBα and RSK1. Our results identify a specific substrate for SGK1 and may facilitate detection of additional physiological substrates for this enzyme.

AB - 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 PKBα or RSK1 in vitro. The inability of PKBα 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 PKBα and RSK1. Our results identify a specific substrate for SGK1 and may facilitate detection of additional physiological substrates for this enzyme.

KW - NDRG1

KW - PKB

KW - Protein kinase specificity

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JO - FEBS Letters

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Identification of different specificity requirements between SGK1 and PKBα

Abstract

Keywords

ASJC Scopus subject areas

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