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.

Proteomics unravels the exportability of mitochondrial respiratory chains

PANFOLI, ISABELLA;RAVERA, SILVIA;MORELLI, ALESSANDRO
2011

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.
File in questo prodotto:
File Dimensione Formato  
Expert Review Proteomics_2011.pdf

accesso chiuso

Tipologia: Documento in versione editoriale
Dimensione 375.9 kB
Formato Unknown
375.9 kB Unknown   Visualizza/Apri   Richiedi una copia

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/11567/254571
Citazioni
  • ???jsp.display-item.citation.pmc??? 14
  • Scopus 49
  • ???jsp.display-item.citation.isi??? 45
social impact