Calcium/calmodulin-dependent protein kinase type II subunit alpha (CAMKIIα), a.k.a. Ca2+/calmodulin-dependent protein kinase II alpha, is one subunit of CamKII, a protein kinase (i.e., an enzyme which phosphorylatesproteins) that in humans is encoded by the CAMK2Agene.[5][6]
The product of the CAMK2A gene is an enzyme that belongs to the serine/threonine-specific protein kinase family, as well as the Ca2+/calmodulin-dependent protein kinase II subfamily. Ca2+ signaling is crucial for several aspects of synaptic plasticity at glutamatergic synapses. This enzyme is composed of four different chains: alpha, beta, gamma, and delta. The alpha chain encoded by this gene is required for hippocampal long-term potentiation (LTP) and spatial learning.[citation needed] In addition to its calcium-calmodulin (CaM)-dependent activity, this protein can undergo autophosphorylation, resulting in CaM-independent activity. Two transcript variants encoding distinct isoforms have been identified for this gene.[7] According to a 2018 study by Bruno Reversade, the recessive mutation of CAMK2A in humans cause a syndrome of severe intellectual disability with growth retardation.[8]
^"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.
^Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, et al. (February 1999). "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Research. 6 (1): 63–70. doi:10.1093/dnares/6.1.63. PMID10231032.
Soderling TR (June 2000). "CaM-kinases: modulators of synaptic plasticity". Current Opinion in Neurobiology. 10 (3): 375–80. doi:10.1016/S0959-4388(00)00090-8. PMID10851169. S2CID31122499.
Hook SS, Means AR (2001). "Ca(2+)/CaM-dependent kinases: from activation to function". Annual Review of Pharmacology and Toxicology. 41 (1): 471–505. doi:10.1146/annurev.pharmtox.41.1.471. PMID11264466.
Yamamoto H (March 2002). "[Molecular mechanisms of the intracellular localizations of Ca2+/calmodulin-dependent protein kinase II isoforms, and their physiological functions]". Tanpakushitsu Kakusan Koso. Protein, Nucleic Acid, Enzyme. 47 (3): 241–7. PMID11889801.
Tokui T, Yamauchi T, Yano T, Nishi Y, Kusagawa M, Yatani R, Inagaki M (June 1990). "Ca2(+)-calmodulin-dependent protein kinase II phosphorylates various types of non-epithelial intermediate filament proteins". Biochemical and Biophysical Research Communications. 169 (3): 896–904. doi:10.1016/0006-291X(90)91977-Z. PMID2114109.
Tsujimura K, Tanaka J, Ando S, Matsuoka Y, Kusubata M, Sugiura H, et al. (August 1994). "Identification of phosphorylation sites on glial fibrillary acidic protein for cdc2 kinase and Ca(2+)-calmodulin-dependent protein kinase II". Journal of Biochemistry. 116 (2): 426–34. doi:10.1093/oxfordjournals.jbchem.a124542. PMID7822264.
Rotenberg A, Mayford M, Hawkins RD, Kandel ER, Muller RU (December 1996). "Mice expressing activated CaMKII lack low frequency LTP and do not form stable place cells in the CA1 region of the hippocampus". Cell. 87 (7): 1351–61. doi:10.1016/S0092-8674(00)81829-2. PMID8980240. S2CID16704390.
Paudel HK (January 1997). "The regulatory Ser262 of microtubule-associated protein tau is phosphorylated by phosphorylase kinase". The Journal of Biological Chemistry. 272 (3): 1777–85. doi:10.1074/jbc.272.3.1777 (inactive 31 May 2021). PMID8999860.CS1 maint: DOI inactive as of May 2021 (link)
External links[]
Human CAMK2A genome location and CAMK2A gene details page in the UCSC Genome Browser.