Journal article
Identification of a Human Akt3 (Protein Kinase B γ) Which Contains the Regulatory Serine Phosphorylation Site
Biochemical and biophysical research communications, Vol.257(3), pp.906-910
04/21/1999
DOI: 10.1006/bbrc.1999.0559
PMID: 10208883
Abstract
The family of protein kinases called Akt, protein kinase B (PKB), or related to A and C kinase (RAC) have been implicated in numerous biological processes including adipocyte and muscle differentiation, glycogen synthesis, glucose uptake, apoptosis and cellular proliferation. There are 3 known isoforms of this enzyme in mammalian cells (1/α, 2/β and 3/γ). Akt1 and 2 contain a key regulatory serine phosphorylation site in the carboxy-terminal region of the protein. However, the reported sequence of the rat Akt3 protein differed significantly from this in that it lacked 25 amino acids in the C-terminal region, including this key regulatory serine phosphorylation site (Biochem. Biophys. Res. Commun.216, 526–534). In the present studies we show that the deduced sequence of human Akt3 contains this serine and that it is phosphorylated in response to insulin. These results indicate that human Akt3 is regulated similarly to Akt1 and Akt2.
Details
- Title: Subtitle
- Identification of a Human Akt3 (Protein Kinase B γ) Which Contains the Regulatory Serine Phosphorylation Site
- Creators
- Kaname Nakatani - Department of Molecular Pharmacology, Stanford University School of Medicine, Stanford, California, 94305Hiroshi Sakaue - Department of Molecular Pharmacology, Stanford University School of Medicine, Stanford, California, 94305Devon A Thompson - Department of Surgery, Stanford University School of Medicine, Stanford, California, 94305Ronald J Weigel - Department of Surgery, Stanford University School of Medicine, Stanford, California, 94305Richard A Roth - Department of Molecular Pharmacology, Stanford University School of Medicine, Stanford, California, 94305
- Resource Type
- Journal article
- Publication Details
- Biochemical and biophysical research communications, Vol.257(3), pp.906-910
- Publisher
- Elsevier Inc
- DOI
- 10.1006/bbrc.1999.0559
- PMID
- 10208883
- ISSN
- 0006-291X
- eISSN
- 1090-2104
- Language
- English
- Date published
- 04/21/1999
- Academic Unit
- Molecular Physiology and Biophysics; Anatomy and Cell Biology; Surgery; Biochemistry and Molecular Biology
- Record Identifier
- 9984024503702771
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