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Assessment of Sarcoplasmic Reticulum Calcium Reserve and Intracellular Diastolic Calcium Removal in Isolated Ventricular Cardiomyocytes
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Protein kinase D regulates the human cardiac L-type voltage-gated calcium channel through serine 1884

Yusuke Aita1, Nagomi Kurebayashi, Shigehisa Hirose

  • 1Department of Biological Sciences, Tokyo Institute of Technology, Yokohama, Japan.

FEBS Letters
|November 22, 2011
PubMed

Insights

Protein kinase D (PKD) regulates human L-type calcium channels. Serine 1884 is identified as a crucial phosphorylation site essential for this PKD regulation, impacting channel activity.

Area of Science:

  • Cardiovascular Physiology
  • Molecular Cell Biology
  • Ion Channel Function

Background:

  • Protein kinase D (PKD) is known to modulate L-type calcium channel activity.
  • The specific functional residues targeted by PKD on the L-type calcium channel have not been identified.

Purpose of the Study:

  • To identify the functional phosphorylation sites of PKD on the human L-type calcium channel (hCaV1.2).

Main Methods:

  • Stable expression of the human CaV1.2 pore subunit in HEK293 cells.
  • Utilized a dominant-negative mutant of PKD and site-directed mutagenesis of serine residues (S1884, S1930).
  • Measured L-type calcium currents and single channel activity, assessed channel expression at the plasma membrane.

Main Results:

  • Mutation of serine 1884, but not serine 1930, significantly reduced L-type calcium currents and single channel activity.
  • The observed reduction in channel activity was independent of changes in channel expression at the plasma membrane.
  • Inhibition of endogenous PKD activity using a dominant-negative mutant also decreased channel currents.

Conclusions:

  • Serine 1884 is a critical functional phosphorylation site for PKD regulation of the human L-type calcium channel (hCaV1.2).
  • PKD-mediated phosphorylation at S1884 is essential for normal L-type calcium channel function.

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