[HTML][HTML] Identification of palmitoylation sites within the L-type calcium channel β2a subunit and effects on channel function
The hydrophilic β 2a subunit of the L-type calcium channel was recently shown to be a
membrane-localized, post-translationally modified protein (Chien, AJ, Zhao, XL, Shirokov,
RE, Puri, TS, Chang, CF, Sun, DD, Rios, E., and Hosey, MM (1995) J. Biol. Chem. 270,
30036-30044). In this study, we demonstrate that the rat β 2a subunit was palmitoylated
through a hydroxylamine-sensitive thioester linkage. Palmitoylation required a pair of
cysteines in the N terminus, Cys 3 and Cys 4; mutation of these residues to serines resulted …
membrane-localized, post-translationally modified protein (Chien, AJ, Zhao, XL, Shirokov,
RE, Puri, TS, Chang, CF, Sun, DD, Rios, E., and Hosey, MM (1995) J. Biol. Chem. 270,
30036-30044). In this study, we demonstrate that the rat β 2a subunit was palmitoylated
through a hydroxylamine-sensitive thioester linkage. Palmitoylation required a pair of
cysteines in the N terminus, Cys 3 and Cys 4; mutation of these residues to serines resulted …