Mechanisms for association of Ca2+/calmodulin-dependent protein kinase II with lipid rafts.
Localization of CaMKIIalpha in lipid rafts was demonstrated in both cultured neurons and mammalian cells transfected with plasmid with an insert of CaMKIIalpha cDNA by using sucrose gradient centrifugation and the sensitivity to a cholesterol-extractor, methyl-beta-cyclodextrin. CaMKIIalpha was targeted to lipid rafts possibly through protein-protein interactions via at least three domains (a.a. 261-309, 371-420, and 421-478). The multimeric structure of the full-length molecule also appeared to contribute to efficient lipid raft-targeting. Acylation of CaMKIIalpha did not appear to be a mechanism for the targeting.
Du
Feng
F
Department of Neuroplasticity, Research Institute on Aging and Adaptation, Shinshu University Graduate School of Medicine, Matsumoto, Japan.
Saitoh
Fuminori
F
Tian
Qing-Bao
QB
Miyazawa
Shoko
S
Endo
Shogo
S
Suzuki
Tatsuo
T
D000818:Animals; D019556:COS Cells; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000235:genetics / Q000378:metabolism*; D002458:Cell Fractionation; D002522:Chlorocebus aethiops; D019811:Hydroxylamine / Q000494:pharmacology; D021962:Membrane Microdomains / Q000187:drug effects / Q000201:enzymology*; D010769:Phosphothreonine / Q000378:metabolism; D011485:Protein Binding; D051381:Rats
D010769:Phosphothreonine; D019811:Hydroxylamine; D054732:Calcium-Calmodulin-Dependent Protein Kinase Type 2; D017871:Calcium-Calmodulin-Dependent Protein Kinases