N-terminus oligomerization is conserved in intracellular calcium release channels

作者：Zissimopoulos Spyros^*; Marsh Jason; Stannard Laurence; Seidel Monika; Lai F Anthony

来源：Biochemical Journal, 2014, 459(2): 265-273.

DOI：10.1042/BJ20131061

• inositol 1, 4, 5-trisphosphate receptor
• intracellular calcium release channel
• N-terminus
• ryanodine receptor
• tetramerization

Oligomerization of all three mammalian ryanodine receptor isoforms, a structural requirement for normal intracellular Ca2+ release channel function, is displayed by the discrete N-terminal domain which assembles into homo- and hetero-tetramers. This is demonstrated in yeast, mammalian cells and native tissue by complementary yeast two-hybrid, chemical cross-linking and co-immunoprecipitation assays. The IP3 (inositol 1,4,5-trisphosphate) receptor N-terminus (residues 1-667) similarly exhibits tetrameric association as indicated by chemical cross-linking and co-immunoprecipitation assays. The presence of either a 15-residue splice insertion or of the cognate ligand IP3 did not affect tetramerization of the IP3 receptor N-terminus. Thus N-terminus tetramerization appears to be an essential intrinsic property that is conserved in both the ryanodine receptor and IP3 receptor families of mammalian intracellular Ca2+ release channels.

• 出版日期2014-4-15