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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
1997-12-9
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pubmed:abstractText |
To acquire information on the relationships between structural maturation of proteins in the endoplasmic reticulum (ER) and their transport along the secretory pathway, we have analyzed the destiny of an assembly-defective form of the trimeric vacuolar storage glycoprotein phaseolin. In leaves of transgenic tobacco, where assembly-competent phaseolin is correctly targeted to the vacuole, defective phaseolin remains located in the ER or a closely related compartment where it represents a major ligand of the chaperone BiP. Defective phaseolin maintained susceptibility to endoglycosidase H and was slowly degraded by a process that is not inhibited by heat shock or brefeldin A, indicating that degradation does not involve transport along the secretory pathway. These results provide evidence for the presence of a quality control mechanism in the ER of plant cells that avoids intracellular trafficking of severely defective proteins and eventually leads to their degradation.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-11184457,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-1344885,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-1498598,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-1511140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-16664795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-16665338,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-1722459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-1822990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-1893109,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-2509938,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-2997710,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-3654619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-7495572,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-7640527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-7647686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-8223484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-8269947,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-8531801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-8580763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-8582868,
http://linkedlifedata.com/resource/pubmed/commentcorrection/9368420-8989886
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1040-4651
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1869-80
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pubmed:dateRevised |
2010-9-13
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pubmed:meshHeading |
pubmed-meshheading:9368420-Biological Transport,
pubmed-meshheading:9368420-Cell Compartmentation,
pubmed-meshheading:9368420-Endoplasmic Reticulum,
pubmed-meshheading:9368420-Golgi Apparatus,
pubmed-meshheading:9368420-Hydrolysis,
pubmed-meshheading:9368420-Molecular Chaperones,
pubmed-meshheading:9368420-Plant Proteins,
pubmed-meshheading:9368420-Plants, Genetically Modified,
pubmed-meshheading:9368420-Plants, Toxic,
pubmed-meshheading:9368420-Protein Processing, Post-Translational,
pubmed-meshheading:9368420-Tobacco,
pubmed-meshheading:9368420-Vacuoles
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pubmed:year |
1997
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pubmed:articleTitle |
Protein quality control along the route to the plant vacuole.
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pubmed:affiliation |
Istituto Biosintesi Vegetali, Consiglio Nazionale delle Ricerche, Milan, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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