Proteomics unravels the exportability of mitochondrial respiratory chains

Isabella Panfoli, Silvia Ravera, Maurizio Bruschi, Giovanni Candiano, Alessandro Morelli

Research output: Contribution to journalArticle

Abstract

Expression of F1Fo-ATP synthase, which generates the majority of cellular ATP and is believed to be strictly confined to mitochondria, has recently been identified in ectopic locations, together with the four complexes of oxidative phosphorylation (OXPHOS) or enzymes from the Krebs cycle. Identification of these proteins has mostly been accomplished by proteomic methods and mass spectrometry - techniques that hold great promise in increasing our understanding of the proteome. The ectopic presence of ATP synthase has variably been attributed to contamination of the sample or to its action as a cell-surface receptor for apparently unrelated ligands, but OXPHOS proteins have sometimes been found to be catalytically active in oxidative phosphorylation, as they were true components of the system under investigation. The present article focuses on how mass spectrometry can increase our understanding of the proteome of subcellular membranes. We review the recent evidence for an extra-mitochondrial expression of OXPHOS by proteomics studies, highlighting what we can learn by combining these data.

Original languageEnglish
Pages (from-to)231-239
Number of pages9
JournalExpert Review of Proteomics
Volume8
Issue number2
DOIs
Publication statusPublished - Apr 2011

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Keywords

  • extra-mitochondrial OXPHOS activity
  • F1Fo-ATP synthase
  • Kreb's cycle
  • lipid raft
  • mitochondrial complexes
  • proteomic analyses
  • subcellular membrane

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry

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