Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2001-6-4
pubmed:abstractText
One challenge facing eukaryotic cells is the post-translational import of proteins into organelles. This problem is exacerbated when the proteins assemble into large complexes. Aminopeptidase I (API) is a resident hydrolase of the vacuole/lysosome in the yeast Saccharomyces cerevisiae. The precursor form of API assembles into a dodecamer in the cytosol and maintains this oligomeric form during the import process. Vacuolar delivery of the precursor form of API requires a vesicular mechanism termed the cytoplasm to vacuole targeting (Cvt) pathway. Many components of the Cvt pathway are also used in the degradative autophagy pathway. alpha-Mannosidase (Ams1) is another resident hydrolase that enters the vacuole independent of the secretory pathway; however, its mechanism of vacuolar delivery has not been established. We show vacuolar localization of Ams1 is blocked in mutants that are defective in the Cvt and autophagy pathways. We have found that Ams1 forms an oligomer in the cytoplasm. The oligomeric form of Ams1 is also detected in subvacuolar vesicles in strains that are blocked in vesicle breakdown, indicating that it retains its oligomeric form during the import process. These results identify Ams1 as a second biosynthetic cargo protein of the Cvt and autophagy pathways.
pubmed:grant
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10233148, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10233150, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10339815, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10511706, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10547367, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10607655, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10662773, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10677852, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10681575, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10837477, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10966461, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10966464, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-10995454, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-11038174, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-11085977, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-11086004, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-11100732, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-11149920, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-11157979, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-11208131, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-11309418, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-1400574, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-1400575, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-2211613, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-2266133, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-2659436, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-3028648, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-3033651, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-3062374, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-3281936, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-350285, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-7533169, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-7593182, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-7962087, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-8663607, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-8670153, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-8901576, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-9151668, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-9188496, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-9214379, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-9224897, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-9412464, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-9451011, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-9712845, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-9759731, http://linkedlifedata.com/resource/pubmed/commentcorrection/11264288-9852036
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
8
pubmed:volume
276
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
20491-8
pubmed:dateRevised
2011-9-26
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Vacuolar localization of oligomeric alpha-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae.
pubmed:affiliation
Department of Biology, University of Michigan, Ann Arbor, Michigan 48109, USA.
pubmed:publicationType
Journal Article
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