Membrane Targeting of L-type Calcium Channels

摘要: In this study, we report that palmitoylation was a critical determinant of the subcellular localization rat beta2a subunit voltage-dependent calcium channels. Immunohistochemical staining transfected cells revealed palmitoylation-deficient exhibited diffuse intracellular pattern, in contrast to plasma membrane distribution seen with wild-type subunit. Unexpectedly, mutations regions distal sites at Cys3 and Cys4 affected protein. Mutations an src homology 3 motif both A mutation beta interaction domain, which disrupted interactions between expressed alpha1 subunits, also resulted decreased Studies chimeric proteins 16-amino acid N terminus sufficient confer nonpalmitoylated beta1b beta3 isoforms. However, subunits by itself insufficient restore observed Treatment brefeldin increased amount palmitic incorporated protein, suggesting occurs during or shortly after protein synthesis. Two other beta2 variants, rabbit beta2b, lack sties Cys4, pattern were not palmitoylated.