Source:http://linkedlifedata.com/resource/pubmed/id/12482753
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
9
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| pubmed:dateCreated |
2003-2-24
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| pubmed:abstractText |
We examined the effects of protein folding on endoplasmic reticulum (ER)-to-cytosol transport (dislocation) by exploiting the well-characterized dihydrofolate reductase (DHFR) domain. DHFR retains the capacity to bind folate analogues in the lumen of microsomes and in the ER of intact cells, upon which it acquires a conformation resistant to proteinase K digestion. Here we show that a Class I major histocompatibility complex heavy chain fused to DHFR is still recognized by the human cytomegalovirus-encoded glycoproteins US2 and US11, resulting in dislocation of the fusion protein from the ER in vitro and in vivo. A folded state of the DHFR domain does not impair dislocation of Class I MHC heavy chains in vitro or in living cells. In fact, a slight acceleration of the dislocation of DHFR heavy chain fusion was observed in vitro in the presence of a folate analogue. These results suggest that one or more of the channels used for dislocation can accommodate polypeptides that contain a tightly folded domain of considerable size. Our data raise the possibility that the Sec61 channel can be modified to accommodate a folded DHFR domain for dislocation, but not for translocation into the ER, or that a channel altogether distinct from Sec61 is used for dislocation.
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| pubmed:grant | |
| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidase K,
http://linkedlifedata.com/resource/pubmed/chemical/Folic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SEC61 protein
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| pubmed:status |
MEDLINE
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| pubmed:month |
Feb
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
28
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| pubmed:volume |
278
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| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
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| pubmed:pagination |
6664-72
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| pubmed:dateRevised |
2007-11-14
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| pubmed:meshHeading |
pubmed-meshheading:12482753-Cytosol,
pubmed-meshheading:12482753-DNA, Complementary,
pubmed-meshheading:12482753-Endopeptidase K,
pubmed-meshheading:12482753-Endoplasmic Reticulum,
pubmed-meshheading:12482753-Folic Acid,
pubmed-meshheading:12482753-Humans,
pubmed-meshheading:12482753-Membrane Proteins,
pubmed-meshheading:12482753-Microsomes,
pubmed-meshheading:12482753-Protein Binding,
pubmed-meshheading:12482753-Protein Biosynthesis,
pubmed-meshheading:12482753-Protein Conformation,
pubmed-meshheading:12482753-Protein Folding,
pubmed-meshheading:12482753-Protein Structure, Tertiary,
pubmed-meshheading:12482753-Protein Transport,
pubmed-meshheading:12482753-RNA, Messenger,
pubmed-meshheading:12482753-Recombinant Fusion Proteins,
pubmed-meshheading:12482753-Subcellular Fractions,
pubmed-meshheading:12482753-Transcription, Genetic,
pubmed-meshheading:12482753-Transfection,
pubmed-meshheading:12482753-Tumor Cells, Cultured
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| pubmed:year |
2003
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| pubmed:articleTitle |
Protein unfolding is not a prerequisite for endoplasmic reticulum-to-cytosol dislocation.
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| pubmed:affiliation |
Department of Pathology, Harvard Medical School, Boston, Massachusetts 02115, USA.
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| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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