Mechanisms for association of Ca2+/calmodulin-dependent protein kinase II with lipid rafts
Localization of CaMKIIα in lipid rafts was demonstrated in both cultured neurons and mammalian cells transfected with plasmid with an insert of CaMKIIα cDNA by using sucrose gradient centrifugation and the sensitivity to a cholesterol-extractor, methyl-β-cyclodextrin. CaMKIIα was targeted to lipid r...
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Veröffentlicht in: | Biochemical and biophysical research communications 2006-09, Vol.347 (3), p.814-820 |
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Hauptverfasser: | , , , , , |
Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | Localization of CaMKIIα in lipid rafts was demonstrated in both cultured neurons and mammalian cells transfected with plasmid with an insert of CaMKIIα cDNA by using sucrose gradient centrifugation and the sensitivity to a cholesterol-extractor, methyl-β-cyclodextrin. CaMKIIα 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 CaMKIIα did not appear to be a mechanism for the targeting. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1016/j.bbrc.2006.06.162 |