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Cellular functions of immunophilins

A R Marks1

  • 1Laboratory of Molecular Cardiology, Cardiovascular Institute, Department of Medicine, Mount Sinai School of Medicine, New York, USA.

Physiological Reviews
|July 1, 1996
PubMed
Summary

Immunophilins are conserved proteins with peptidyl-prolyl isomerase activity. Their precise cellular functions, beyond drug interactions, remain largely unknown, though some modulate calcium release channels.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cellular Biology

Background:

  • Immunophilins are a conserved protein family characterized by cis-trans peptidyl-prolyl isomerase activity.
  • Prototypic immunophilins, cyclophilin A and FKBP12, bind immunosuppressive drugs like cyclosporin, FK506, and rapamycin.
  • The immunosuppressive effects are mediated by drug binding, not the isomerase activity itself, leaving the enzymatic function's role unclear.

Purpose of the Study:

  • To explore the cellular functions of immunophilins beyond their interaction with immunosuppressive drugs.
  • To investigate the role of immunophilin prolyl isomerase activity in cellular processes.
  • To understand the broader biological significance of this conserved protein family.

Main Methods:

  • Literature review and analysis of existing research on immunophilins.
  • Examination of protein expression patterns and tissue distribution.
  • Case study analysis of specific immunophilins with identified cellular roles.

Main Results:

  • The prolyl isomerase activity of immunophilins is not essential for their immunosuppressive drug-mediated effects.
  • The specific cellular roles of most immunophilins remain largely undefined.
  • FKBP12 and FKBP12.6 modulate intracellular calcium release channel function, independent of immunosuppressive ligands.

Conclusions:

  • Despite conserved prolyl isomerase activity, the primary cellular functions of many immunophilins are obscure.
  • FKBP12 and FKBP12.6 serve as integral components of calcium release channel complexes (ryanodine receptors and IP3 receptor).
  • FKBP12 and FKBP12.6 may enhance channel function by increasing subunit cooperativity, highlighting a defined cellular role.

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