N-terminus oligomerization is conserved in intracellular calcium release channels

9Citations
Citations of this article
5Readers
Mendeley users who have this article in their library.

Abstract

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free