| pubmed-article:9794811 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9794811 | lifeskim:mentions | umls-concept:C0005528 | lld:lifeskim |
| pubmed-article:9794811 | lifeskim:mentions | umls-concept:C1327616 | lld:lifeskim |
| pubmed-article:9794811 | lifeskim:mentions | umls-concept:C0041217 | lld:lifeskim |
| pubmed-article:9794811 | pubmed:dateCreated | 1998-12-28 | lld:pubmed |
| pubmed-article:9794811 | pubmed:abstractText | We have investigated the role of glycosylphosphatidylinositol (GPI) anchors in forward secretory trafficking using African trypanosomes as a model system. Soluble GPI-minus forms of variant surface glycoprotein (VSG), in which the C-terminal GPI-addition peptide signal is deleted, are secreted from transformed procyclic trypanosomes with 5-fold reduced kinetics, relative to matched GPI-anchored constructs. Cell fractionation and immunofluorescence localization studies indicate that the GPI-minus VSG reporters accumulate in the endoplasmic reticulum (ER). This transport defect is specific, since overexpression of GPI-minus VSG has no effect on the rate of transport of a second soluble secretory reporter (BiPN) when co-expressed in the same cells. Two results suggest that delayed forward transport cannot be accounted for by failure to fold/assemble in the absence of a GPI anchor, thereby leading to prolonged association with ER quality-control machinery. First, no evidence was found for elevated association of GPI-minus VSG with the ER molecular chaperone, BiP. Secondly, newly synthesized GPI-minus VSG is dimerized efficiently, as judged by velocity-sedimentation analysis. GPI-dependent transport is not confined to the VSG reporters, because a similar dependence is found with another trypanosomal GPI-anchored protein, trans-sialidase. These findings suggest that GPI structures act in a positive manner to mediate efficient forward transport of some, and perhaps all, GPI-anchored proteins in the early secretory pathway of trypanosomes. Possible mechanisms for GPI-dependent transport are discussed with respect to current models of vesicular trafficking. | lld:pubmed |
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| pubmed-article:9794811 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9794811 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9794811 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9794811 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9794811 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:9794811 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:9794811 | pubmed:author | pubmed-author:BangsJ DJD | lld:pubmed |
| pubmed-article:9794811 | pubmed:author | pubmed-author:RansonD LDL | lld:pubmed |
| pubmed-article:9794811 | pubmed:author | pubmed-author:McDowellM AMA | lld:pubmed |
| pubmed-article:9794811 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9794811 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9794811 | pubmed:volume | 335 ( Pt 3) | lld:pubmed |
| pubmed-article:9794811 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9794811 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9794811 | pubmed:pagination | 681-9 | lld:pubmed |
| pubmed-article:9794811 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:9794811 | pubmed:meshHeading | pubmed-meshheading:9794811-... | lld:pubmed |
| pubmed-article:9794811 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9794811 | pubmed:articleTitle | Glycosylphosphatidylinositol-dependent secretory transport in Trypanosoma brucei. | lld:pubmed |
| pubmed-article:9794811 | pubmed:affiliation | Department of Medical Microbiology and Immunology, University of Wisconsin-Madison Medical School, 1300 University Avenue, Madison, WI 53706, USA. | lld:pubmed |
| pubmed-article:9794811 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9794811 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9794811 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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