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Control of a novel adenylyl cyclase by calcineurin

J M Paterson1, S M Smith, A J Harmar

  • 1MRC Brain Metabolism Unit, University of Edinburgh, Scotland, UK.

Insights

The immunosuppressant FK506 and FKBP12 protein complex inhibits calcineurin. A novel calcineurin-regulated adenylyl cyclase with an FKBP12-like domain may be a physiological target for these drugs.

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Pharmacology

Background:

  • The immunosuppressant FK506 forms a complex with FKBP12, inhibiting calcineurin, a Ca2+/calmodulin-activated protein phosphatase.
  • This inhibition mechanism is conserved across cell types, suggesting exploitation of fundamental calcineurin regulation by immunosuppressants.

Purpose of the Study:

  • To identify novel physiological targets of calcineurin.
  • To investigate the role of calcineurin in neuronal function.

Main Methods:

  • Identification and characterization of a novel adenylyl cyclase.
  • Analysis of enzyme messenger RNA distribution and localization in the brain.

Main Results:

  • A novel adenylyl cyclase regulated by calcineurin was discovered.
  • This enzyme possesses an FKBP12-like domain, suggesting it could be a physiological calcineurin binding site.
  • The enzyme's mRNA is highly expressed in the cerebral cortex, striatum, and hippocampus, localizing to neuronal perikarya.

Conclusions:

  • The novel adenylyl cyclase represents a potential physiological target mimicked by immunosuppressant-immunophilin complexes.
  • Its enrichment in specific brain regions suggests a significant role in neuronal function and regulation.

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