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

J J MacKrill1

  • 1Department of Biochemistry, University College Cork, National University of Ireland, Cork, Ireland.

The Biochemical Journal
|January 23, 1999
PubMed
Summary

Calcium-release channels (CRCs), including inositol 1,4, 5-trisphosphate receptors (InsP3Rs) and ryanodine receptors (RyRs), are regulated by accessory proteins. This review details how these interactions customize CRC function in cells.

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Calcium ions (Ca2+) are critical intracellular messengers.
  • Ca2+ release channels, such as inositol 1,4, 5-trisphosphate receptors (InsP3Rs) and ryanodine receptors (RyRs), control Ca2+ release from intracellular stores.
  • These channels are modulated by numerous accessory proteins, influencing cellular signaling.

Purpose of the Study:

  • To review the regulation of Ca2+-release channel (CRC) activity by accessory proteins.
  • To outline the structural details of protein-protein interactions modulating CRC function.
  • To provide a comprehensive survey of CRC-interacting proteins.

Main Methods:

  • Literature review of existing research on CRCs and their accessory proteins.

Related Experiment Videos

  • Analysis of structural and functional data regarding protein-protein interactions.
  • Synthesis of information on the modulatory roles of accessory proteins.

    • Main Results:

    • Accessory proteins interact with InsP3Rs and RyRs, modulating their channel activity.
    • Regulation can be class-specific, isoform-specific, or affect all CRC subtypes.
    • Some accessory proteins are sensitive to Ca2+ concentrations, creating feedback loops.

    Conclusions:

    • Accessory proteins critically 'customize' the function of InsP3Rs and RyRs in specific cellular contexts.
    • These interactions allow CRCs to integrate diverse signaling events.
    • Understanding these protein-protein interactions is key to comprehending cellular Ca2+ signaling.