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PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2006-2-27
pubmed:abstractText
Bro1-domain proteins such as yeast Bro1 and mammalian AIP1/Alix are well-established participants in endosome metabolism. The Bro1-domain interacts with endosomal surface protein Snf7/Vps32 in yeast, a subunit of the ESCRT complex. Yeast Bro1-domain protein Rim20 has no role in endosome function, but is required for alkaline pH-stimulated cleavage of transcription factor Rim101. Rim20-GFP is cytoplasmic under acidic conditions but concentrated in punctate foci under alkaline conditions. Bro1-GFP also accumulates in foci, but they are more numerous under acidic than alkaline conditions. Colocalization experiments indicate that some Rim20-GFP foci correspond to Bro1-RFP foci, whereas others do not. Rim8, Rim9, Rim21, Dfg16, Snf7, Vps20, Vps23, and Vps25, which are required for Rim101 cleavage, are required for appearance of Rim20-GFP foci. ESCRT complexes accumulate on endosome-derived compartments in cells that lack the AAA-ATPase Vps4. We find that Rim20-GFP foci accumulate in a vps4 mutant background independently of external pH, Rim101 pathway-specific genes, and most ESCRT subunit genes except for SNF7. Rim20-GFP foci seem to represent endosomes, because they colocalize with Snf7-RFP and because they correspond to a perivacuolar compartment in the vps4 strain. We propose that alkaline growth conditions alter the endosomal surface to favor Rim20-Snf7 interaction and Rim101 cleavage. Our findings raise the possibility that Bro1-domain proteins may be differentially regulated in the same cell, thereby coupling endosome metabolism to signaling.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-10873832, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-11029042, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-11050096, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-11251082, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-11283351, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-11461694, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-11698381, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-12194857, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-12208998, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-12509465, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-12588984, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-12621426, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-12668726, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-12860994, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-12892785, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-14505569, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-14505570, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-14562095, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-14583093, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-14739459, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-15326198, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-15371534, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-15511219, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-15569240, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-15590834, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-15879523, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-15935782, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-16024810, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-16099830, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-16227598, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-16272384, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-16299290, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-7533169, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-9017390, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-9155008, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-9606181, http://linkedlifedata.com/resource/pubmed/commentcorrection/16407402-9928935
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Bro1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Endosomal Sorting Complexes..., http://linkedlifedata.com/resource/pubmed/chemical/NHX1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RIM101 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SNF7 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sodium-Hydrogen Antiporter, http://linkedlifedata.com/resource/pubmed/chemical/Vesicular Transport Proteins
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1059-1524
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1344-53
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed-meshheading:16407402-Cation Transport Proteins, pubmed-meshheading:16407402-DNA-Binding Proteins, pubmed-meshheading:16407402-Endocytosis, pubmed-meshheading:16407402-Endosomal Sorting Complexes Required for Transport, pubmed-meshheading:16407402-Hydrogen-Ion Concentration, pubmed-meshheading:16407402-Models, Biological, pubmed-meshheading:16407402-Mutation, pubmed-meshheading:16407402-Nuclear Proteins, pubmed-meshheading:16407402-Protein Structure, Tertiary, pubmed-meshheading:16407402-Protein Transport, pubmed-meshheading:16407402-Recombinant Fusion Proteins, pubmed-meshheading:16407402-Repressor Proteins, pubmed-meshheading:16407402-Saccharomyces cerevisiae, pubmed-meshheading:16407402-Saccharomyces cerevisiae Proteins, pubmed-meshheading:16407402-Sodium-Hydrogen Antiporter, pubmed-meshheading:16407402-Transport Vesicles, pubmed-meshheading:16407402-Vacuoles, pubmed-meshheading:16407402-Vesicular Transport Proteins
pubmed:year
2006
pubmed:articleTitle
Control of Bro1-domain protein Rim20 localization by external pH, ESCRT machinery, and the Saccharomyces cerevisiae Rim101 pathway.
pubmed:affiliation
Integrated Program in Cellular, Molecular, and Biophysical Studies, Columbia University, New York, NY 10032, USA.
pubmed:publicationType
Journal Article
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