Mitochondrial porin links protein biogenesis to metabolism

Curr Genet. 2019 Aug;65(4):899-903. doi: 10.1007/s00294-019-00965-z. Epub 2019 Apr 3.

Abstract

In this report, we summarize recent findings about a role of the outer membrane metabolite channel VDAC/porin in protein import into mitochondria. Mitochondria fulfill key functions for cellular energy metabolism. Their biogenesis involves the import of about 1000 different proteins that are produced as precursors on cytosolic ribosomes. The translocase of the outer membrane (TOM complex) forms the entry gate for mitochondrial precursor proteins. Dedicated protein translocases sort the preproteins into the different mitochondrial subcompartments. While protein transport pathways are analyzed to some detail, only little is known about regulatory mechanisms that fine-tune protein import upon metabolic signaling. Recently, a dual role of the voltage-dependent anion channel (VDAC), also termed porin, in mitochondrial protein biogenesis was reported. First, VDAC/porin promotes as a coupling factor import of carrier proteins into the inner membrane. Second, VDAC/porin regulates the formation of the TOM complex. Thus, the major metabolite channel in the outer membrane VDAC/porin connects protein import to mitochondrial metabolism.

Keywords: Mitochondria; Protein import; TOM complex; VDAC.

Publication types

  • Review

MeSH terms

  • Carrier Proteins / genetics
  • Cytosol / metabolism
  • Energy Metabolism / genetics*
  • Mitochondria / genetics*
  • Mitochondrial Membranes / metabolism
  • Mitochondrial Precursor Protein Import Complex Proteins
  • Mitochondrial Proteins / genetics*
  • Mitochondrial Proteins / metabolism
  • Organelle Biogenesis*
  • Protein Transport / genetics
  • Ribosomes / genetics
  • Saccharomyces cerevisiae / genetics
  • Voltage-Dependent Anion Channels / genetics

Substances

  • Carrier Proteins
  • Mitochondrial Precursor Protein Import Complex Proteins
  • Mitochondrial Proteins
  • Voltage-Dependent Anion Channels