rdf:type |
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lifeskim:mentions |
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pubmed:issue |
8
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pubmed:dateCreated |
2010-8-10
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pubmed:abstractText |
The GET pathway, using several proteins (Gets 1-5 and probably Sgt2), posttranslationally conducts tail-anchored (TA) proteins to the endoplasmic reticulum (ER). At the ER, TA proteins are inserted into the lipid bilayer and then sorted and directed to their respective destinations in the secretory pathway. Until last year, there was no structural information on any of the GET components but now there are ten crystal structures of Get3 in a variety of nucleotide-bound states and conformations. The structures of Get4 and a portion of Get5 also emerged in 2010. This minireview provides a detailed comparison of the GET structures and discusses their mechanistic relevance to TA protein insertion. It also addresses the outstanding gaps in detailed molecular information on this system, including the structures of Get5, Sgt2, and the transmembrane complex comprising Get1 and Get2.
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pubmed:grant |
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GET4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Get3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Exchange Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Mdy2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1878-4186
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pubmed:author |
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pubmed:copyrightInfo |
Copyright 2010 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
11
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
897-902
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pubmed:meshHeading |
pubmed-meshheading:20696390-Adenosine Triphosphatases,
pubmed-meshheading:20696390-Carrier Proteins,
pubmed-meshheading:20696390-Endoplasmic Reticulum,
pubmed-meshheading:20696390-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:20696390-Models, Biological,
pubmed-meshheading:20696390-Models, Molecular,
pubmed-meshheading:20696390-Protein Transport,
pubmed-meshheading:20696390-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:20696390-Signal Transduction,
pubmed-meshheading:20696390-Ubiquitin
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pubmed:year |
2010
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pubmed:articleTitle |
Structures of Get3, Get4, and Get5 provide new models for TA membrane protein targeting.
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pubmed:affiliation |
Division of Molecular Biosciences, Imperial College London, Exhibition Road, South Kensington, London SW7 2AZ, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Review,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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