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Related Experiment Videos

PKA holoenzyme is functionally coupled to CFTR by AKAPs.

P Huang1, K Trotter, R C Boucher

  • 1Departments of Medicine and CF/Pulmonary Research and Treatment Center, University of North Carolina, Chapel Hill, North Carolina 27599, USA. Pingbo_Huang@med.unc.edu

American Journal of Physiology. Cell Physiology
|February 9, 2000
PubMed
Summary

A kinase anchoring proteins (AKAPs) tether protein kinase A (PKA) to the cystic fibrosis transmembrane regulator (CFTR). This AKAP-PKA-CFTR complex is crucial for CFTR regulation by physiological stimuli.

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • The cystic fibrosis transmembrane regulator (CFTR) is a crucial ion channel.
  • Membrane-bound protein kinase A (PKAII) is thought to regulate CFTR.
  • A kinase anchoring proteins (AKAPs) are known to localize PKA to specific cellular sites.

Purpose of the Study:

  • To investigate the physical and functional association between PKA and CFTR.
  • To determine the role of AKAPs in PKA-CFTR complex formation and CFTR regulation.

Main Methods:

  • Utilized inside-out membrane patches from Calu-3 cells.
  • Applied 8-(4-chlorophenylthio)adenosine 3',5'-cyclic monophosphate (CPT-cAMP) and PKI to assess PKA activity.
  • Used HT-31 peptide to disrupt AKAP-PKA interactions.

Related Experiment Videos

  • Conducted whole-cell voltage-clamp studies with intracellular dialysis.

    • Main Results:

    • Isolated Calu-3 membrane patches contained functional PKA holoenzyme coupled to CFTR.
    • CPT-cAMP significantly increased CFTR activity, an effect blocked by PKI.
    • HT-31 disrupted PKA-CFTR coupling and prevented CPT-cAMP-mediated CFTR activation in patches.
    • HT-31 blocked CFTR activation by extracellular adenosine in whole-cell studies.

    Conclusions:

    • AKAPs mediate the compartmentalization of PKA holoenzyme with CFTR in Calu-3 cells.
    • AKAP-dependent PKA localization is essential for the physiological regulation of CFTR.