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Titolo:
Protein-protein interactions in intracellular Ca2+-release channel function
Autore:
Mackrill, JJ;
Indirizzi:
Natl Univ Ireland Univ Coll Cork, Dept Biochem, Cork, Ireland Natl Univ Ireland Univ Coll Cork Cork Ireland pt Biochem, Cork, Ireland
Titolo Testata:
BIOCHEMICAL JOURNAL
, volume: 337, anno: 1999,
parte:, 3
pagine: 345 - 361
SICI:
0264-6021(19990201)337:<345:PIIICC>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
INOSITOL 1,4,5-TRISPHOSPHATE RECEPTOR; CA2+ RELEASE CHANNEL; JUNCTIONAL SARCOPLASMIC-RETICULUM; CARDIAC RYANODINE RECEPTOR; RABBIT SKELETAL-MUSCLE; AMP-DEPENDENT PHOSPHORYLATION; RECONSTITUTED LIPID VESICLES; FK506 BINDING-PROTEIN; T-LYMPHOMA CELLS; II-III LOOP;
Keywords:
accessory proteins; inositol 1,4,5,-trisphosphate; receptor; ryanodine receptor;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
219
Recensione:
Indirizzi per estratti:
Indirizzo: Mackrill, JJ Natl Univ Ireland Univ Coll Cork, Dept Biochem, Cork, IrelandNatl Univ Ireland Univ Coll Cork Cork Ireland ork, Ireland
Citazione:
J.J. Mackrill, "Protein-protein interactions in intracellular Ca2+-release channel function", BIOCHEM J, 337, 1999, pp. 345-361

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 (InsP(3)Rs) and the ryanodine receptors (RyRs). Multiple isoforms andsubtypes of each CRC class display distinct but overlapping distributions within mammalian tissues. InsP(3)Rs 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 rolesof these modulators. The aim of this article is to review the regulation of CRC activity by accessory proteins and, wherever possible, to outline thestructural details of such interactions. The CRCs are large transmembrane proteins, with the bulk of their structure located cytoplasmically. Intra- and inter-complex protein-protein inter-actions between these cytoplasmic domains also regulate CRC function. Some accessory proteins modulate channelactivity 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 InsP(3)R 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 InsP(3)Rs and RyRs within particular cells and subcellular domains are 'customized' by the accessory proteins present.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 21:42:35