*Wales Heart Research Institute, Cardiff University School of Medicine, Institute of Molecular and Experimental Medicine, Heath Park, Cardiff CF14 4XN, U.K.
Biochem J. 2014 Apr 15;459(2):265-73. doi: 10.1042/BJ20131061.
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.
三种哺乳动物兰尼碱受体异构体的寡聚化是正常细胞内 Ca2+释放通道功能的结构要求，由离散的 N 端结构域组成同源和异源四聚体来显示。这在酵母、哺乳动物细胞和天然组织中通过互补酵母双杂交、化学交联和共免疫沉淀实验得到证实。IP3（肌醇 1,4,5-三磷酸）受体 N 端（残基 1-667）也表现出四聚体缔合，如化学交联和共免疫沉淀实验所示。15 个残基的剪接插入或同源配体 IP3 的存在并不影响 IP3 受体 N 端的四聚化。因此，N 端四聚化似乎是一种内在的基本特性，在哺乳动物细胞内 Ca2+释放通道的兰尼碱受体和 IP3 受体家族中都得到了保守。
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