PKB binding proteins. Getting in on the Akt
- PMID: 12419241
- DOI: 10.1016/s0092-8674(02)01083-8
PKB binding proteins. Getting in on the Akt
Abstract
Protein kinase B (PKB) has emerged as the focal point for many signal transduction pathways, regulating multiple cellular processes such as glucose metabolism, transcription, apoptosis, cell proliferation, angiogenesis, and cell motility. In addition to acting as a kinase toward many substrates involved in these processes, PKB forms complexes with other proteins that are not substrates, but rather act as modulators of PKB activity and function. In this review, we discuss the implications of these data in understanding the multitude of functions predicted for PKB in cells.
Similar articles
-
Stabilization of Mdm2 via decreased ubiquitination is mediated by protein kinase B/Akt-dependent phosphorylation.J Biol Chem. 2004 Aug 20;279(34):35510-7. doi: 10.1074/jbc.M404936200. Epub 2004 May 28. J Biol Chem. 2004. PMID: 15169778
-
Protein kinase B phosphorylation of PIKfyve regulates the trafficking of GLUT4 vesicles.J Cell Sci. 2004 Dec 1;117(Pt 25):5985-93. doi: 10.1242/jcs.01517. Epub 2004 Nov 16. J Cell Sci. 2004. PMID: 15546921
-
Involvement of the Akt/PKB signaling pathway with disease processes.Mol Cell Biochem. 2003 Nov;253(1-2):241-6. doi: 10.1023/a:1026020101379. Mol Cell Biochem. 2003. PMID: 14619975 Review.
-
Cross-talk between Akt, p53 and Mdm2: possible implications for the regulation of apoptosis.Oncogene. 2002 Feb 14;21(8):1299-303. doi: 10.1038/sj.onc.1205181. Oncogene. 2002. PMID: 11850850
-
The regulation and activities of the multifunctional serine/threonine kinase Akt/PKB.Exp Cell Res. 1999 Nov 25;253(1):210-29. doi: 10.1006/excr.1999.4690. Exp Cell Res. 1999. PMID: 10579924 Review.
Cited by
-
K63-linked ubiquitination in kinase activation and cancer.Front Oncol. 2012 Jan 31;2:5. doi: 10.3389/fonc.2012.00005. eCollection 2012. Front Oncol. 2012. PMID: 22649774 Free PMC article.
-
SILAM for quantitative proteomics of liver Akt1/PKBα after burn injury.Int J Mol Med. 2012 Mar;29(3):461-71. doi: 10.3892/ijmm.2011.861. Epub 2011 Dec 14. Int J Mol Med. 2012. PMID: 22179310 Free PMC article.
-
Gαo potentiates estrogen receptor α activity via the ERK signaling pathway.J Endocrinol. 2012 Jul;214(1):45-54. doi: 10.1530/JOE-12-0097. Epub 2012 May 4. J Endocrinol. 2012. PMID: 22562654 Free PMC article.
-
Y box-binding protein 1 induces resistance to oncogenic transformation by the phosphatidylinositol 3-kinase pathway.Proc Natl Acad Sci U S A. 2003 Oct 14;100(21):12384-9. doi: 10.1073/pnas.2135336100. Epub 2003 Oct 6. Proc Natl Acad Sci U S A. 2003. PMID: 14530393 Free PMC article.
-
Ceramide disables 3-phosphoinositide binding to the pleckstrin homology domain of protein kinase B (PKB)/Akt by a PKCzeta-dependent mechanism.Mol Cell Biol. 2003 Nov;23(21):7794-808. doi: 10.1128/MCB.23.21.7794-7808.2003. Mol Cell Biol. 2003. PMID: 14560023 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Miscellaneous