PRKCB1
In this article, we will explore PRKCB1 from different perspectives, analyzing its impact on today's society and its relevance in history. With a critical and objective look, we will address the most important aspects related to PRKCB1, delving into its origins, evolution and development over time. Through a thorough analysis, we will unravel the different concepts and theories that revolve around PRKCB1, with the purpose of providing a comprehensive understanding of its importance in the contemporary context. In addition, we will examine the implications and effects that PRKCB1 has had in various areas, thus allowing a broad and detailed vision of its significance today.
Protein kinase C beta type is an enzyme that in humans is encoded by the PRKCB gene.[5]
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.[6] This gene could be associated with autism.[7][8]
Interactions
PRKCB1 has been shown to interact with RIPK4,[9] beta adrenergic receptor kinase,[10] PDLIM5[11] and GNB2L1.[12]
See also
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000166501 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000052889 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Kubo K, Ohno S, Suzuki K (September 1987). "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. doi:10.1093/nar/15.17.7179. PMC 306204. PMID 3658678.
- ^ "Entrez Gene: PRKCB1 protein kinase C, beta 1".
- ^ Philippi A, Roschmann E, Tores F, Lindenbaum P, Benajou A, Germain-Leclerc L, et al. (October 2005). "Haplotypes in the gene encoding protein kinase c-beta (PRKCB1) on chromosome 16 are associated with autism". Molecular Psychiatry. 10 (10): 950–60. doi:10.1038/sj.mp.4001704. PMID 16027742.
- ^ Lintas C, Sacco R, Garbett K, Mirnics K, Militerni R, Bravaccio C, et al. (July 2009). "Involvement of the PRKCB1 gene in autistic disorder: significant genetic association and reduced neocortical gene expression". Molecular Psychiatry. 14 (7): 705–18. doi:10.1038/mp.2008.21. PMID 18317465.
- ^ Chen L, Haider K, Ponda M, Cariappa A, Rowitch D, Pillai S (June 2001). "Protein kinase C-associated kinase (PKK), a novel membrane-associated, ankyrin repeat-containing protein kinase". The Journal of Biological Chemistry. 276 (24): 21737–44. doi:10.1074/jbc.M008069200. PMID 11278382.
- ^ Yang XL, Zhang YL, Lai ZS, Xing FY, Liu YH (April 2003). "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. doi:10.3748/wjg.v9.i4.800. PMC 4611453. PMID 12679936.
- ^ Kuroda S, Tokunaga C, Kiyohara Y, Higuchi O, Konishi H, Mizuno K, et al. (December 1996). "Protein-protein interaction of zinc finger LIM domains with protein kinase C". The Journal of Biological Chemistry. 271 (49): 31029–32. doi:10.1074/jbc.271.49.31029. PMID 8940095.
- ^ Ron D, Jiang Z, Yao L, Vagts A, Diamond I, Gordon A (September 1999). "Coordinated movement of RACK1 with activated betaIIPKC". The Journal of Biological Chemistry. 274 (38): 27039–46. doi:10.1074/jbc.274.38.27039. PMID 10480917.
Further reading
- Mochly-Rosen D (April 1995). "Localization of protein kinases by anchoring proteins: a theme in signal transduction". Science. 268 (5208): 247–51. Bibcode:1995Sci...268..247M. doi:10.1126/science.7716516. PMID 7716516.
- Ali A, Hoeflich KP, Woodgett JR (August 2001). "Glycogen synthase kinase-3: properties, functions, and regulation". Chemical Reviews. 101 (8): 2527–40. doi:10.1021/cr000110o. PMID 11749387.
- Slater SJ, Ho C, Stubbs CD (June 2002). "The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions". Chemistry and Physics of Lipids. 116 (1–2): 75–91. doi:10.1016/S0009-3084(02)00021-X. PMID 12093536.
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