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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
2006-3-13
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pubmed:abstractText |
During encystation Giardia trophozoites secrete a fibrillar extracellular matrix of glycans and cyst wall proteins on the cell surface. The cyst wall material is accumulated in encystation-specific vesicles (ESVs), specialized Golgi-like compartments generated de novo, after export from the endoplasmic reticulum (ER) and before secretion. These large post-ER vesicles neither have the morphological characteristics of Golgi cisternae nor sorting functions, but may represent an evolutionary early form of the Golgi-like maturation compartment. Because little is known about the genesis and maturation of ESVs, we used a limited proteomics approach to discover novel proteins that are specific for developing ESVs or associated peripherally with these organelles. Unexpectedly, we identified cytoplasmic and luminal factors of the ER quality control system on two-dimensional electrophoresis gels, i.e. several proteasome subunits and HSP70-BiP. We show that BiP is exported to ESVs and retrieved via its C-terminal KDEL signal from ESVs. In contrast, cytoplasmic proteasome complexes undergo a developmentally regulated re-localization to ESVs during encystation. This suggests that maturation of bulk exported cyst wall material in the Golgi-like ESVs involves both continuous activity of ER-associated quality control mechanisms and retrograde Golgi to ER transport.
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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/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Dithiothreitol,
http://linkedlifedata.com/resource/pubmed/chemical/Genetic Markers,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Sucrose,
http://linkedlifedata.com/resource/pubmed/chemical/molecular chaperone GRP78
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
281
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7595-604
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16407213-Animals,
pubmed-meshheading:16407213-Blotting, Western,
pubmed-meshheading:16407213-Centrifugation, Density Gradient,
pubmed-meshheading:16407213-Cytoplasm,
pubmed-meshheading:16407213-Disulfides,
pubmed-meshheading:16407213-Dithiothreitol,
pubmed-meshheading:16407213-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:16407213-Endoplasmic Reticulum,
pubmed-meshheading:16407213-Genetic Markers,
pubmed-meshheading:16407213-Genetic Vectors,
pubmed-meshheading:16407213-Giardia lamblia,
pubmed-meshheading:16407213-Golgi Apparatus,
pubmed-meshheading:16407213-HSP70 Heat-Shock Proteins,
pubmed-meshheading:16407213-Heat-Shock Proteins,
pubmed-meshheading:16407213-Mass Spectrometry,
pubmed-meshheading:16407213-Microscopy,
pubmed-meshheading:16407213-Microsomes,
pubmed-meshheading:16407213-Models, Biological,
pubmed-meshheading:16407213-Molecular Chaperones,
pubmed-meshheading:16407213-Mutation,
pubmed-meshheading:16407213-Nucleic Acids,
pubmed-meshheading:16407213-Open Reading Frames,
pubmed-meshheading:16407213-Polysaccharides,
pubmed-meshheading:16407213-Proteasome Endopeptidase Complex,
pubmed-meshheading:16407213-Protein Structure, Tertiary,
pubmed-meshheading:16407213-Proteomics,
pubmed-meshheading:16407213-Recombinant Proteins,
pubmed-meshheading:16407213-Subcellular Fractions,
pubmed-meshheading:16407213-Sucrose,
pubmed-meshheading:16407213-Time Factors,
pubmed-meshheading:16407213-Transgenes
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pubmed:year |
2006
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pubmed:articleTitle |
Organelle proteomics reveals cargo maturation mechanisms associated with Golgi-like encystation vesicles in the early-diverged protozoan Giardia lamblia.
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pubmed:affiliation |
Institute of Parasitology, University of Zürich, Winterthurerstrasse 266a, CH-8057 Zürich, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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