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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2005-8-1
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pubmed:abstractText |
Peroxisomal import receptors bind their cargo proteins in the cytosol and target them to docking and translocation machinery at the peroxisomal membrane (reviewed in ref. 1). The receptors release the cargo proteins into the peroxisomal lumen and, according to the model of cycling receptors, they are supposed to shuttle back to the cytosol. This shuttling of the receptors has been assigned to peroxins including the AAA peroxins Pex1p and Pex6p, as well as the ubiquitin-conjugating enzyme Pex4p (reviewed in ref. 2). One possible target for Pex4p is the PTS1 receptor Pex5p, which has recently been shown to be ubiquitinated. Pex1p and Pex6p are both cytosolic and membrane-associated AAA ATPases of the peroxisomal protein import machinery, the exact function of which is still unknown. Here we demonstrate that the AAA peroxins mediate the ATP-dependent dislocation of the peroxisomal targeting signal-1 (PTS1) receptor from the peroxisomal membrane to the cytosol.
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Leupeptins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/PEX1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/PEX15 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/PEX6 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cytoplasmic and Nuclear,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/benzyloxycarbonylleucyl-leucyl-leuci...,
http://linkedlifedata.com/resource/pubmed/chemical/peroxisome-targeting signal 1...
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1465-7392
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
817-22
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pubmed:dateRevised |
2007-11-19
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pubmed:meshHeading |
pubmed-meshheading:16007078-Adenosine Triphosphatases,
pubmed-meshheading:16007078-Adenosine Triphosphate,
pubmed-meshheading:16007078-Cell Fractionation,
pubmed-meshheading:16007078-Cysteine Proteinase Inhibitors,
pubmed-meshheading:16007078-Cytosol,
pubmed-meshheading:16007078-Fungal Proteins,
pubmed-meshheading:16007078-Intracellular Membranes,
pubmed-meshheading:16007078-Leupeptins,
pubmed-meshheading:16007078-Membrane Proteins,
pubmed-meshheading:16007078-Multiprotein Complexes,
pubmed-meshheading:16007078-Mutation,
pubmed-meshheading:16007078-Peroxisomes,
pubmed-meshheading:16007078-Phosphoproteins,
pubmed-meshheading:16007078-Proteasome Endopeptidase Complex,
pubmed-meshheading:16007078-Protein Transport,
pubmed-meshheading:16007078-Receptors, Cytoplasmic and Nuclear,
pubmed-meshheading:16007078-Saccharomyces cerevisiae,
pubmed-meshheading:16007078-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:16007078-Ubiquitin
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pubmed:year |
2005
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pubmed:articleTitle |
Functional role of the AAA peroxins in dislocation of the cycling PTS1 receptor back to the cytosol.
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pubmed:affiliation |
Institut für Physiologische Chemie, Abt. Systembiochemie, Ruhr-Universität Bochum, D-44780 Bochum, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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