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. 2023 Jan 23;12(3):401. doi: 10.3390/cells12030401

Table 2.

Proteins that alter their binding to CaMKII in response to changes in CaMKII phosphorylation.

Binding Partner Effect of CaMKII Phosphorylation/Phospho-Mimic Mutation on Binding Ref
Protein Cellular Function
Brain and acute leukaemia (BAALC) 1-6-8 Haematopoietic cell proliferation, survival, and differentiation Non-phosphorylated and 286 phospho-mimic mutants bind, 253 phospho-mimic mutation significantly increases binding [93,96]
Calcium channel α-subunit isoforms (L-type) Calcium influx Non-phosphorylated CaMKII binds α1, α2a, α3 and α4 subunits; pThr286 binds only α1 and α2a subunits [97]
Camguk/CASK Synaptic targeting and synaptic plasticity Non-phosphorylated CaMKII binds, pThr305/306 decreases binding [95]
Densin-180 (LRRC7) Dendritic scaffolding protein pThr286 enhances binding compared to non-phosphorylated CaMKII [98,99]
Desmin Muscle intermediate filament Non-phosphorylated CaMKII binds, 286 and 253 phospho-mimic mutations increase binding [91,92,93]
Diacylglycerol lipase α (DGLα) Key enzyme in biosynthesis of the endocannabinoid 2-arachidonoylglycerol Non-phosphorylated CaMKII does not bind, pT286 directly interacts [100]
Metabotropic glutamate receptor 5 (mGluR5) Metabotropic glutamate receptor involved in various brain functions, including motor behaviour, memory and cognition pT286 decreases binding compared to non-phosphorylated CaMKII [101]
Microtubule-associated protein 2 (MAP-2) Microtubule assembly Non-phosphorylated CaMKII binds, 286 phospho-mimic mutation increases binding [91,92,93]
Myelin Basic Protein (MBP) Major component of the myelin sheath Non-phosphorylated CaMKII binds, 286 phospho-mimic mutation slightly decreases binding, 253 phospho-mimic mutation abrogates binding [93]
GRIN2A/2B
(GluN2A/2B)
Subunit of voltage-sensitive ionotropic glutamate receptor involved in synaptic plasticity pThr286 enhances binding compared to non-phosphorylated CaMKII [85,86,87,88]
Projectin Integral protein of insect flight muscle pThr286 decreases binding compared to non-phosphorylated CaMKII [102]
Syntaxin 1A Component of exocytotic molecular machinery Non-phosphorylated CaMKII did not bind, pT286 directly interacts [103]
Tau Microtubule assembly Non-phosphorylated and 253 phospho-mimic mutation bind, 286 phospho-mimic mutation increases binding [92,93,104]
Tyrosine hydroxylase isoform 2 (human) Catecholamine biosynthesis Non-phosphorylated and 286 phospho-mimic mutants bind, 253 phospho-mimic mutation increases binding [93]
Tyrosine hydroxylase isoform 2 (human), phosphorylated at Ser19 and Ser40 Catecholamine biosynthesis Binding is enhanced for non-phosphorylated, 286 and 253 phospho-mimic mutation when compared to non-phosphorylated tyrosine hydroxylase [93]