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IP(3) receptors: toward understanding their activation.

Colin W Taylor1, Stephen C Tovey

  • 1Department of Pharmacology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1PD, United Kingdom. cwt1000@cam.ac.uk

Cold Spring Harbor Perspectives in Biology
|October 29, 2010
PubMed
Summary

Inositol 1,4,5-trisphosphate receptors (IP(3)R) release calcium ions from intracellular stores. This review explores how IP(3) and calcium binding activate IP(3)R structure, influencing calcium signaling pathways.

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Published on: June 8, 2022

Area of Science:

  • Molecular Biology
  • Cellular Physiology
  • Biochemistry

Background:

  • Inositol 1,4,5-trisphosphate receptors (IP(3)R) and ryanodine receptors are key channels for intracellular calcium (Ca2+) release.
  • These receptors regulate Ca2+ signaling and can propagate signals regeneratively through Ca2+ binding.

Purpose of the Study:

  • To review the structural basis of IP(3)R activation by IP(3) and Ca2+.
  • To elucidate the mechanism of IP(3)-mediated Ca2+ release and signal propagation.

Main Methods:

  • Structural analysis of IP(3)R.
  • Review of existing literature on IP(3)R function and regulation.
  • Hypothesizing structural interactions during IP(3)R activation.

Main Results:

  • IP(3) binding promotes Ca2+ binding to a stimulatory site, initiating IP(3)R activation.
  • The IP(3)-binding core closes upon phosphate group interactions, inducing conformational changes.
  • A pore structure with a selectivity filter and gate controls cation flux.

Conclusions:

  • The N-terminal suppressor domain mediates conformational changes from the IP(3)-binding core to the pore.
  • The pore's luminal selectivity filter and cytosolic gate regulate Ca2+ flux through IP(3)R.
  • Understanding IP(3)R structure is crucial for deciphering Ca2+ signaling mechanisms.