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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
35
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pubmed:dateCreated |
2009-10-6
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pubmed:databankReference |
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pubmed:abstractText |
The Get3 ATPase directs the delivery of tail-anchored (TA) proteins to the endoplasmic reticulum (ER). TA-proteins are characterized by having a single transmembrane helix (TM) at their extreme C terminus and include many essential proteins, such as SNAREs, apoptosis factors, and protein translocation components. These proteins cannot follow the SRP-dependent co-translational pathway that typifies most integral membrane proteins; instead, post-translationally, these proteins are recognized and bound by Get3 then delivered to the ER in the ATP dependent Get pathway. To elucidate a molecular mechanism for TA protein binding by Get3 we have determined three crystal structures in apo and ADP forms from Saccharomyces cerevisae (ScGet3-apo) and Aspergillus fumigatus (AfGet3-apo and AfGet3-ADP). Using structural information, we generated mutants to confirm important interfaces and essential residues. These results point to a model of how Get3 couples ATP hydrolysis to the binding and release of TA-proteins.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-10407274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-10708766,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-10970874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-11395509,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-11473577,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-12675792,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-12680698,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-1529353,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-16269340,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-1655273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-17086205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-17289575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-17382883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-17401378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-17419726,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-17629691,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-17681537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-18000004,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-1824941,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-18477612,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-18724936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-19325107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-2406906,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-8445645,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-8923743,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-9002525,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-9163420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-9219684,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/19706470-9677296
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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 |
Sep
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pubmed:issn |
1091-6490
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
106
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
14849-54
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pubmed:dateRevised |
2010-9-27
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pubmed:meshHeading |
pubmed-meshheading:19706470-Adenosine Triphosphatases,
pubmed-meshheading:19706470-Aspergillus fumigatus,
pubmed-meshheading:19706470-Crystallography, X-Ray,
pubmed-meshheading:19706470-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:19706470-Membrane Fusion Proteins,
pubmed-meshheading:19706470-Models, Molecular,
pubmed-meshheading:19706470-Nucleic Acid Conformation,
pubmed-meshheading:19706470-Nucleotides,
pubmed-meshheading:19706470-Phenotype,
pubmed-meshheading:19706470-Protein Binding,
pubmed-meshheading:19706470-Protein Structure, Quaternary,
pubmed-meshheading:19706470-Protein Structure, Tertiary,
pubmed-meshheading:19706470-Saccharomyces cerevisiae,
pubmed-meshheading:19706470-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:19706470-Structural Homology, Protein
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pubmed:year |
2009
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pubmed:articleTitle |
Model for eukaryotic tail-anchored protein binding based on the structure of Get3.
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pubmed:affiliation |
Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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