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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2006-2-1
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pubmed:abstractText |
The recruitment of the small GTPase Arf6 and ARNO from cytosol to endosomal membranes is driven by V-ATPase-dependent intra-endosomal acidification. The molecular mechanism that mediates this pH-sensitive recruitment and its role are unknown. Here, we demonstrate that Arf6 interacts with the c-subunit, and ARNO with the a2-isoform of V-ATPase. The a2-isoform is targeted to early endosomes, interacts with ARNO in an intra-endosomal acidification-dependent manner, and disruption of this interaction results in reversible inhibition of endocytosis. Inhibition of endosomal acidification abrogates protein trafficking between early and late endosomal compartments. These data demonstrate the crucial role of early endosomal acidification and V-ATPase/ARNO/Arf6 interactions in the regulation of the endocytic degradative pathway. They also indicate that V-ATPase could modulate membrane trafficking by recruiting and interacting with ARNO and Arf6; characteristics that are consistent with the role of V-ATPase as an essential component of the endosomal pH-sensing machinery.
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pubmed:grant |
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP-Ribosylation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/ADP-ribosylation factor 6,
http://linkedlifedata.com/resource/pubmed/chemical/Ammonium Chloride,
http://linkedlifedata.com/resource/pubmed/chemical/Carbonyl Cyanide...,
http://linkedlifedata.com/resource/pubmed/chemical/Dynamins,
http://linkedlifedata.com/resource/pubmed/chemical/GTPase-Activating Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Macrolides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Albumin, Bovine,
http://linkedlifedata.com/resource/pubmed/chemical/Vacuolar Proton-Translocating...,
http://linkedlifedata.com/resource/pubmed/chemical/bafilomycin A,
http://linkedlifedata.com/resource/pubmed/chemical/cytohesin-2
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1465-7392
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pubmed:author |
pubmed-author:AusielloDennis ADA,
pubmed-author:BechouaShalihaS,
pubmed-author:BourgoinSylvainS,
pubmed-author:BrownDennisD,
pubmed-author:CasanovaJamesJ,
pubmed-author:El AnnanJaafarJ,
pubmed-author:FutaiMasamitsuM,
pubmed-author:Hurtado-LorenzoAndrésA,
pubmed-author:MarshanskyVladimirV,
pubmed-author:SkinnerMhairiM,
pubmed-author:Sun-WadaGe-HongGH,
pubmed-author:WildemanAlanA
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pubmed:issnType |
Print
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pubmed:volume |
8
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
124-36
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pubmed:dateRevised |
2010-10-11
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pubmed:meshHeading |
pubmed-meshheading:16415858-ADP-Ribosylation Factors,
pubmed-meshheading:16415858-Ammonium Chloride,
pubmed-meshheading:16415858-Animals,
pubmed-meshheading:16415858-Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone,
pubmed-meshheading:16415858-Cell Line,
pubmed-meshheading:16415858-Dynamins,
pubmed-meshheading:16415858-Endocytosis,
pubmed-meshheading:16415858-Endosomes,
pubmed-meshheading:16415858-Epithelial Cells,
pubmed-meshheading:16415858-GTPase-Activating Proteins,
pubmed-meshheading:16415858-Green Fluorescent Proteins,
pubmed-meshheading:16415858-HeLa Cells,
pubmed-meshheading:16415858-Humans,
pubmed-meshheading:16415858-Hydrogen-Ion Concentration,
pubmed-meshheading:16415858-Isoenzymes,
pubmed-meshheading:16415858-Kidney Tubules, Proximal,
pubmed-meshheading:16415858-Macrolides,
pubmed-meshheading:16415858-Mice,
pubmed-meshheading:16415858-Models, Biological,
pubmed-meshheading:16415858-Mutation,
pubmed-meshheading:16415858-Protein Binding,
pubmed-meshheading:16415858-Protein Interaction Mapping,
pubmed-meshheading:16415858-Protein Transport,
pubmed-meshheading:16415858-Proteins,
pubmed-meshheading:16415858-Serum Albumin, Bovine,
pubmed-meshheading:16415858-Transfection,
pubmed-meshheading:16415858-Vacuolar Proton-Translocating ATPases
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pubmed:year |
2006
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pubmed:articleTitle |
V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway.
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pubmed:affiliation |
Program in Membrane Biology & Nephrology Division, Richard Simches Research Center, Massachusetts General Hospital and Department of Medicine, Harvard Medical School, Boston, MA 02114, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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