Protein–protein interactions in intracellular Ca2+-release channel function
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چکیده
منابع مشابه
Protein-protein interactions in intracellular Ca2+-release channel function.
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 mod...
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Cells possess multiple intracellular Ca2+-releasing systems. Sea urchin egg homogenates are a well-established model to study intracellular Ca2+ release. In the present study the mechanism of interaction between three intracellular Ca2+ pools, namely the nicotinic acid adenine dinucleotide phosphate (NAADP), the cyclic ADP-ribose (cADPR) and the inositol 1',4',5'-trisphosphate (IP3)-regulated C...
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Electrical excitation of the mammalian heart originates from specialized pacemaker cells in the right atrium. Pacemaker activity depends on multiple ion channels and transport mechanisms that reside primarily within the plasma membrane. However, recent evidence indicates that intracellular Ca2+ release from the sarcoplasmic reticulum also contributes importantly to atrial pacemaker function.
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13. G. D. Housley and J. F. Ashmore, J. Physiol. (London) 448, 73 (1992). 14. J. F. Ashmore and R. W. Meech, Nature 322, 368 (1986); A. H. Gitter and H. P. Zenner, in Basic Issues in Hearing, H. Duifhuis, J. W. Horst, H. P. Wit, Eds. (Academic Press, London, 1988), pp. 32-39; J. F. Ashmore, in Cochlear Mechanisms, J. P. Wilson and D. T. Kemp, Eds. (Plenum, New York, 1989), pp. 107-113; J. Santo...
متن کاملDivergence of Ca2+ selectivity and equilibrium Ca2+ blockade in a Ca2+ release-activated Ca2+ channel
Prevailing models postulate that high Ca(2+) selectivity of Ca(2+) release-activated Ca(2+) (CRAC) channels arises from tight Ca(2+) binding to a high affinity site within the pore, thereby blocking monovalent ion flux. Here, we examined the contribution of high affinity Ca(2+) binding for Ca(2+) selectivity in recombinant Orai3 channels, which function as highly Ca(2+)-selective channels when ...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1999
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj3370345