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 crosslinking 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. © The Authors Journal compilation © 2014 Biochemical Society.
CITATION STYLE
Zissimopoulos, S., Marsh, J., Stannard, L., Seidel, M., & Lai, F. A. (2014). N-terminus oligomerization is conserved in intracellular calcium release channels. Biochemical Journal, 459(2), 265–273. https://doi.org/10.1042/BJ20131061
Mendeley helps you to discover research relevant for your work.