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PMID: 9895277 Published · ppublish English Journal Article Review

Protein-protein interactions in intracellular Ca2+-release channel function.

The Biochemical journal ·Vol. 337 ( Pt 3) ·1999-02-01 ·Pages 345-61

MacKrill JJ

Abstract

Release of Ca2+ ions from intracellular stores can occur via two classes of Ca2+-release channel (CRC) protein, the inositol 1,4, 5-trisphosphate receptors (InsP3Rs) and the ryanodine receptors (RyRs). Multiple isoforms and subtypes of each CRC class display distinct but overlapping distributions within mammalian tissues. InsP3Rs and RyRs interact with a plethora of accessory proteins which modulate the activity of their intrinsic channels. Although many aspects of CRC structure and function have been reviewed in recent years, the properties of proteins with which they interact has not been comprehensively surveyed, despite extensive current research on the roles of these modulators. The aim of this article is to review the regulation of CRC activity by accessory proteins and, wherever possible, to outline the structural details of such interactions. The CRCs are large transmembrane proteins, with the bulk of their structure located cytoplasmically. Intra- and inter-complex protein-protein interactions between these cytoplasmic domains also regulate CRC function. Some accessory proteins modulate channel activity of all CRC subtypes characterized, whereas other have class- or even isoform-specific effects. Certain accessory proteins exert both direct and indirect forms of regulation on CRCs, occasionally with opposing effects. Others are themselves modulated by changes in Ca2+ concentration, thereby participating in feedback mechanisms acting on InsP3R and RyR activity. CRCs are therefore capable of integrating numerous signalling events within a cell by virtue of such protein-protein interactions. Consequently, the functional properties of InsP3Rs and RyRs within particular cells and subcellular domains are 'customized' by the accessory proteins present.

MeSH Terms
Animals Calcium/metabolism Calcium Channels/physiology Calcium-Binding Proteins/metabolism,physiology Humans Inositol 1,4,5-Trisphosphate/physiology Inositol 1,4,5-Trisphosphate Receptors Membrane Proteins/metabolism,physiology Receptors, Cytoplasmic and Nuclear/physiology Ryanodine Receptor Calcium Release Channel/physiology Subcellular Fractions/metabolism
Chemicals
Calcium Channels Calcium-Binding Proteins ITPR1 protein, human Inositol 1,4,5-Trisphosphate Receptors Membrane Proteins Receptors, Cytoplasmic and Nuclear Ryanodine Receptor Calcium Release Channel Inositol 1,4,5-Trisphosphate Calcium
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
MacKrill J J
Department of Biochemistry, University College Cork, National University of Ireland, Cork, Ireland.
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1999-02-01
Pages
345-61
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1219985
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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