Source:http://linkedlifedata.com/resource/pubmed/id/16269391
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11
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pubmed:dateCreated |
2005-11-4
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pubmed:abstractText |
We have analyzed the functions of two vacuolar t-SNAREs, Vam3p and Vam7p, in peroxisome degradation in the methylotrophic yeast Hansenula polymorpha. A Hp-vam7 mutant was strongly affected in peroxisome degradation by selective macropexophagy as well as non-selective microautophagy. Deletion of Hp-Vam3p function had only a minor effect on peroxisome degradation processes. Both proteins were located at the vacuolar membrane, with Hp-Vam7p also having a partially cytosolic location. Previously, in baker's yeast Vam3p and Vam7p have been demonstrated to be components of a t-SNARE complex essential for vacuole biogenesis. We speculate that the function of this complex in macropexophagy includes a role in membrane fusion processes between the outer membrane layer of sequestered peroxisomes and the vacuolar membrane. Our data suggest that Hp-Vam3p may be functionally redundant in peroxisome degradation. Remarkably, deletion of Hp-VAM7 also significantly affected peroxisome biogenesis and resulted in organelles with multiple, membrane-enclosed compartments. These morphological defects became first visible in cells that were in the mid-exponential growth phase of cultivation on methanol, and were correlated with accumulation of electron-dense extensions that were connected to mitochondria.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Qa-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Qc-SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SNARE Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Synaptosomal-Associated Protein 25,
http://linkedlifedata.com/resource/pubmed/chemical/VAM3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/VAM7 protein, S cerevisiae
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1567-1356
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
985-97
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:16269391-Molecular Sequence Data,
pubmed-meshheading:16269391-Organelles,
pubmed-meshheading:16269391-Peroxisomes,
pubmed-meshheading:16269391-Pichia,
pubmed-meshheading:16269391-Qa-SNARE Proteins,
pubmed-meshheading:16269391-Qc-SNARE Proteins,
pubmed-meshheading:16269391-SNARE Proteins,
pubmed-meshheading:16269391-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:16269391-Synaptosomal-Associated Protein 25,
pubmed-meshheading:16269391-Vacuoles
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pubmed:year |
2005
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pubmed:articleTitle |
Hansenula polymorpha Vam7p is required for macropexophagy.
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pubmed:affiliation |
Eukaryotic Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute (GBB), University of Groningen, P.O. Box 14, 9751 AA Haren, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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