Search results for CAMK2B

Showing 15 results out of 15

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Protein (5 results from a total of 5)

Identifier: R-HSA-9611360
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: Q13554
Identifier: R-HSA-445371
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: CAMK2B: Q13554
Identifier: R-HSA-417009
Species: Homo sapiens
Compartment: endocytic vesicle membrane
Primary external reference: UniProt: CAMK2B: Q13554
Identifier: R-HSA-444787
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: UniProt: CAMK2B: Q13554
Identifier: R-HSA-432791
Species: Homo sapiens
Compartment: plasma membrane
Primary external reference: UniProt: CAMK2B: Q13554

Interactor (1 results from a total of 1)

Identifier: Q13554-3
Species: Homo sapiens
Primary external reference: UniProt: Q13554-3

Set (4 results from a total of 4)

Identifier: R-HSA-9007035
Species: Homo sapiens
Compartment: nucleoplasm
Identifier: R-HSA-432795
Species: Homo sapiens
Compartment: plasma membrane
Identifier: R-HSA-9611359
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9611354
Species: Homo sapiens
Compartment: cytosol

Complex (2 results from a total of 2)

Identifier: R-HSA-9624331
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-9624336
Species: Homo sapiens
Compartment: cytosol

Reaction (3 results from a total of 3)

Identifier: R-HSA-9611368
Species: Homo sapiens
Compartment: cytosol, plasma membrane
The calmodulin-dependent kinase, CaMKII, is enriched in postsynaptic density (PSD) and co-localizes with NMDA receptors. CaMKII can independently bind to alpha-actinin-2 (ACTN2), densin-180 (LRRC7) and the NMDA receptor subunit GluN2B (GRIN2B). Any of the four CAMK2 isoforms, CAMK2A, CAMK2B, CAMK2D or CAMK2G, which associate to form homomeric or heteromeric CaMKII dodecamers, can bind to ACTN2 and GluN2B, while LRRC7 shows the highest affinity for CAMK2A. Binding of CaMKII to the NMDA receptor-associated proteins is independent of CaMKII phosphorylation (Robison et al. 2005).
Identifier: R-HSA-445367
Species: Homo sapiens
Compartment: cytosol, plasma membrane
CaMKII can independentl bind to NMDA receptor-associated proteins alpha-actinin-2 (ACTN2) and densin-180 (LRRC7), as well as the NMDA receptor subunit GluN2B (GRIN2B, NR2B). Any of the four CAMK2 isoforms, CAMK2A, CAMK2B, CAMK2D or CAMK2G, which associate to form homomeric or heteromeric CaMKII dodecamers, can bind to ACTN2 and GluN2B, while LRRC7 shows the highest affinity for CAMK2A (Husi et al. 2000, Robison et al. 2005). Binding of CaMKII to the NMDA receptor-associated proteins is independent of CaMKII phosphorylation (Robinson et al. 2005), but phosphorylation of CaMKII on threonine residue T286 (T287 in CAMK2B, CAMK2D and CAMK2G) is needed for binding to GluN2B (Strack and Colbran 1998, Bayer et al. 2001). Binding to activated calmodulin is needed for translocation of CaMKII from the cytosol to the postsynaptic density (PSD). In the cytosol, CaMKII dodecamers containing CAMK2A subunit bind to F-actin. Dissociation of CAMK2A from F-actin requires either autophosphorylation of CAMK2A or binding to activated calmodulin (Shen and Meyer 1999).
Autophosphorylation increases the affinity of CaMKII for calmodulin and binding of CaMKII to the NMDA receptor subunit GluN2B locks the kinase in an active state, thus prolonging CaMKII signaling (Bayer et al. 2001). Prolonged activity of CaMKII is implicated in long-term potentiation (LTP), which is involved in learning and memory (Fukunaga et al. 1992, Otmakhov et al. 2004). Switching from GluN2B- to GluN2A (GRIN2A)-containing NDMA receptors results in reduced binding of CaMKII to PSD and reduced LTP, which may contribute to reduced synaptic plasticity (Barria and Malinow 2005).
Identifier: R-HSA-5576895
Species: Homo sapiens
Compartment: cytosol, extracellular region, plasma membrane
Sodium channel proteins, subunit alpha (SCNAs) mediate the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na+ ions may pass in accordance with their electrochemical gradient. SCNA channels consist of an ion-conducting, pore-forming alpha-subunit regulated by one or more associated auxiliary subunits SCN1B, 2B, 3B and 4B. SCN1B and 3B are non-covalently associated with SCNA, while SCN2B is covalently linked by disulfide bonds.

SCNAs interact with cytosolic proteins that regulate channel trafficking and/or modulate the biophysical properties of the channels. Fibroblast growth factors (FGFs) are potent regulators of voltage-gated Na+ channels in adult ventricular myocytes and suggest that loss-of-function mutations in FGFs may underlie a similar set of cardiac arrhythmias and cardiomyopathies that result from SCN5A (aka Nav1.5) loss-of-function mutations. Ran guanine nucleotide release factor (RANGRF aka MOG1) is a critical regulator of sodium channel function in the heart and is thought to regulate the cell surface localization of SCN5A (Marfatia et al. 2001, Wu et al. 2008). Calcium/calmodulin-dependent protein kinase type II subunit delta (CAMK2D), as part of a heteromeric complex with CAMK2A, CAMK2B and CAMK2G can be activated by calmodulin/Ca2+ (CALM:4xCa2+) to then phosphorylate SNC5A at multiple sites, inactivating it (Ashpole et al. 2012).
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