Identification of a syntaxin-binding site on N-type calcium channels.
作者： Zu-Hang Sheng , Jens Rettig , Masami Takahashi , William A. Catterall
DOI: 10.1016/0896-6273(94)90417-0
关键词:
摘要: Immunochemical studies have suggested a tight association of syntaxin with N-type calcium channels. Syntaxin specifically interacts the fusion proteins containing cytoplasmic loop (LII-III) between homologous repeats II and III alpha 1 subunit class B channel (alpha 1B) from rat brain, but not those A Q-type 1A) or S L-type 1S) This interaction is mediated by an 87 amino acid sequence (773-859) two overlapping predicted helix-loop-helix domains. The peptide can block binding native channels to syntaxin, indicating that this site required for stable these proteins. Interaction takes place C-terminal one-third (residues 181-288), which thought be anchored in presynaptic plasma membrane. Our results suggest direct domains membrane could important role targeting docking synaptic vesicles near channels, enabling structural functional entry sites neurotransmitter release sites.
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