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The VDAC2-BAK axis regulates peroxisomal membrane permeability

Ken-Ichiro Hosoi1,2, Non Miyata1, Satoru Mukai1

  • 1Department of Biology, Faculty of Sciences, Kyushu University, Nishi-ku, Fukuoka 819-0395, Japan.

The Journal of Cell Biology
|February 9, 2017
PubMed

Insights

Peroxisomal biogenesis disorders involve cell defects. This study reveals VDAC2 influences BAK localization, impacting peroxisome function and permeability, offering new insights into these fatal genetic diseases.

Area of Science:

  • Cell Biology
  • Genetics
  • Biochemistry

Background:

  • Peroxisomal biogenesis disorders (PBDs) are severe genetic conditions affecting cell function.
  • A novel cell mutant, ZP114, was identified as deficient in peroxisome formation and not fitting existing PBD complementation groups.

Purpose of the Study:

  • To identify factors involved in peroxisomal deficiency in the ZP114 cell line.
  • To elucidate the role of BAK in peroxisome function and permeability.

Main Methods:

  • Functional screening to identify VDAC2 as a suppressor of peroxisomal deficiency.
  • Gene knockdown and overexpression studies involving BAK, BCL-XL, MCL-1, PUMA, and BIM.
  • Investigating protein localization shifts (VDAC2, BAK) and peroxisomal protein release.

Main Results:

  • VDAC2 expression rescued peroxisomal deficiency in ZP114 cells, despite not localizing to peroxisomes.
  • Knockdown of BAK or inhibition of BAK restored peroxisomal biogenesis.
  • Loss of VDAC2 caused BAK mislocalization to peroxisomes, leading to deficiency; BAK targeted to peroxisomes caused matrix protein release.
  • BAK activators induced peroxisomal permeabilization.

Conclusions:

  • BAK plays a critical role in regulating peroxisomal permeability.
  • The VDAC2-BAK interaction influences peroxisomal integrity and function.
  • Findings suggest a novel mechanism for controlling peroxisome permeability, analogous to mitochondrial outer membrane permeabilization.

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