N-terminus oligomerization is conserved in intracellular calcium release channels

Zissimopoulos, Spyros, Marsh, Jason, Stannard, Laurence, Seidel, Monika and Lai, Francis ORCID: https://orcid.org/0000-0003-2852-8547 2014. N-terminus oligomerization is conserved in intracellular calcium release channels. Biochemical Journal 459 (2) , pp. 265-273. 10.1042/BJ20131061

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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 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.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Schools > Biosciences Schools > Medicine
Subjects:	R Medicine > R Medicine (General)
Publisher:	Biochemical Society
ISSN:	0264-6021
Last Modified:	28 Oct 2022 10:29
URI:	https://orca.cardiff.ac.uk/id/eprint/78529

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