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]
Function
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]
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.
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]
Function
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]
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.