Biology:PRKCB1
 Generic protein structure example |
Protein kinase C beta type is an enzyme that in humans is encoded by the PRKCB gene.[1]
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported.[2] This gene could be associated with autism.[3][4]
Interactions
PRKCB1 has been shown to interact with RIPK4,[5] beta adrenergic receptor kinase,[6] PDLIM5[7] and GNB2L1.[8]
See also
References
- ↑ "Nucleotide sequence of the 3' portion of a human gene for protein kinase C beta I/beta II". Nucleic Acids Research 15 (17): 7179–80. September 1987. doi:10.1093/nar/15.17.7179. PMID 3658678.
- ↑ "Entrez Gene: PRKCB1 protein kinase C, beta 1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5579.
- ↑ "Haplotypes in the gene encoding protein kinase c-beta (PRKCB1) on chromosome 16 are associated with autism". Molecular Psychiatry 10 (10): 950–60. October 2005. doi:10.1038/sj.mp.4001704. PMID 16027742.
- ↑ "Involvement of the PRKCB1 gene in autistic disorder: significant genetic association and reduced neocortical gene expression". Molecular Psychiatry 14 (7): 705–18. July 2009. doi:10.1038/mp.2008.21. PMID 18317465.
- ↑ "Protein kinase C-associated kinase (PKK), a novel membrane-associated, ankyrin repeat-containing protein kinase". The Journal of Biological Chemistry 276 (24): 21737–44. June 2001. doi:10.1074/jbc.M008069200. PMID 11278382.
- ↑ "Pleckstrin homology domain of G protein-coupled receptor kinase-2 binds to PKC and affects the activity of PKC kinase". World Journal of Gastroenterology 9 (4): 800–3. April 2003. doi:10.3748/wjg.v9.i4.800. PMID 12679936.
- ↑ "Protein-protein interaction of zinc finger LIM domains with protein kinase C". The Journal of Biological Chemistry 271 (49): 31029–32. December 1996. doi:10.1074/jbc.271.49.31029. PMID 8940095.
- ↑ "Coordinated movement of RACK1 with activated betaIIPKC". The Journal of Biological Chemistry 274 (38): 27039–46. September 1999. doi:10.1074/jbc.274.38.27039. PMID 10480917.
Further reading
- "Localization of protein kinases by anchoring proteins: a theme in signal transduction". Science 268 (5208): 247–51. April 1995. doi:10.1126/science.7716516. PMID 7716516. Bibcode: 1995Sci...268..247M.
- "Glycogen synthase kinase-3: properties, functions, and regulation". Chemical Reviews 101 (8): 2527–40. August 2001. doi:10.1021/cr000110o. PMID 11749387.
- "The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions". Chemistry and Physics of Lipids 116 (1–2): 75–91. June 2002. doi:10.1016/S0009-3084(02)00021-X. PMID 12093536.
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