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DPP6 domains responsible for its localization and function.

Lin Lin1, Laura K Long1, Michael M Hatch1

  • 1Molecular Neurophysiology and Biophysics Section, Program in Developmental Neuroscience, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892.

The Journal of Biological Chemistry
|September 6, 2014
PubMed
Summary
This summary is machine-generated.

The cysteine-rich domain of dipeptidyl peptidase-like protein 6 (DPP6) is crucial for its cell surface expression. This domain

Keywords:
Endoplasmic Reticulum (ER)Intracellular TraffickingMembrane TraffickingNeuronNeuronal ExcitabilityPotassium Channeldpp6kv4.2

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Area of Science:

  • Molecular biology
  • Cellular neuroscience
  • Protein biochemistry

Background:

  • Dipeptidyl peptidase-like protein 6 (DPP6) is an auxiliary subunit of Kv4 potassium channels.
  • DPP6 enhances Kv4 channel surface expression and kinetics.
  • DPP6 possesses a large extracellular domain with an uncharacterized cysteine-rich motif.

Purpose of the Study:

  • To investigate the function of the cysteine-rich domain of DPP6.
  • To determine the role of DPP6's cysteine-rich domain in Kv4 channel trafficking and function.

Main Methods:

  • Site-directed mutagenesis to disrupt disulfide bonds in the cysteine-rich domain.
  • Western blotting and immunofluorescence to assess protein expression and localization.
  • Electrophysiological recordings to evaluate Kv4.2 channel kinetics and function.

Main Results:

  • The cysteine-rich domain of DPP6 is essential for its ER export and cell surface expression.
  • Specific disulfide bridges (C349/C356 and C465/C468) within this domain are required for enhancing Kv4.2 surface expression.
  • While intracellular domains interact with Kv4.2 and affect inactivation, the entire extracellular domain is necessary for surface expression and stabilization.

Conclusions:

  • The cysteine-rich domain of DPP6 is critical for proper protein folding, enabling ER export.
  • Disulfide bond formation within the cysteine-rich domain is vital for DPP6's role in Kv4 channel trafficking.
  • DPP6's extracellular domain is key for stabilizing Kv4.2 at the cell surface.