Mitochondrial porin, or VDAC, is a pore-forming protein abundant in the outer mitochondrialmembrane. Several publications have reported extramitochondrial localizations as well, butthe evidence was considered insufficient by many, and the presence of porin in nonmitochondrialcellular compartments has remained in doubt for a long time. We have now obtained newdata indicating that the plasma membrane of hematopoietic cells contains porin, probablylocated mostly in caveolae or caveolae-like domains. Porin was purified from the plasmamembrane of intact cells by a procedure utilizing the membrane-impermeable labeling reagentNH-SS-biotin and streptavidin affinity chromatography, and shown to have the same propertiesas mitochondrial porin. A channel with properties similar to that of isolated VDAC wasobserved by patch-clamping intact cells. This review discusses the evidence supporting extramitochondriallocalization, the putative identification of the plasma membrane porin with the“maxi” chloride channel, the hypothetical mechanisms of sorting porin to various cellularmembrane structures, and its possible functions.

Extramitochondrial porin: facts and hypotheses

MESSINA, Angela Anna;DE PINTO, Vito Nicola;
2000-01-01

Abstract

Mitochondrial porin, or VDAC, is a pore-forming protein abundant in the outer mitochondrialmembrane. Several publications have reported extramitochondrial localizations as well, butthe evidence was considered insufficient by many, and the presence of porin in nonmitochondrialcellular compartments has remained in doubt for a long time. We have now obtained newdata indicating that the plasma membrane of hematopoietic cells contains porin, probablylocated mostly in caveolae or caveolae-like domains. Porin was purified from the plasmamembrane of intact cells by a procedure utilizing the membrane-impermeable labeling reagentNH-SS-biotin and streptavidin affinity chromatography, and shown to have the same propertiesas mitochondrial porin. A channel with properties similar to that of isolated VDAC wasobserved by patch-clamping intact cells. This review discusses the evidence supporting extramitochondriallocalization, the putative identification of the plasma membrane porin with the“maxi” chloride channel, the hypothetical mechanisms of sorting porin to various cellularmembrane structures, and its possible functions.
2000
caveolae; cholesterol transport; patch clamp
File in questo prodotto:
File Dimensione Formato  
49.BB32.79.PDF

solo gestori archivio

Tipologia: Versione Editoriale (PDF)
Licenza: Non specificato
Dimensione 127 kB
Formato Adobe PDF
127 kB Adobe PDF   Visualizza/Apri

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: https://hdl.handle.net/20.500.11769/1006
Citazioni
  • ???jsp.display-item.citation.pmc??? 15
  • Scopus 55
  • ???jsp.display-item.citation.isi??? 50
social impact