Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
13
pubmed:dateCreated
2010-3-22
pubmed:databankReference
pubmed:abstractText
Get3, Get4, and Get5 in Saccharomyces cerevisiae participate in the insertion of tail-anchored proteins into the endoplasmic reticulum membrane. We elucidated the interaction between Get4 and Get5 and investigated their interaction with Get3 and a tetratricopeptide repeat-containing protein, Sgt2. Based on co-immunoprecipitation and crystallographic studies, Get4 and Get5 formed a tight complex, suggesting that they constitute subunits of a larger complex. In contrast, although Get3 interacted physically with the Get4-Get5 complex, low amounts of Get3 co-precipitated with Get5, implying a transient interaction between Get3 and Get4-Get5. Sgt2 also interacted with Get5, although the amount of Sgt2 that co-precipitated with Get5 varied. Moreover, GET3, GET4, and GET5 interacted genetically with molecular chaperone YDJ1, suggesting that chaperones might also be involved in the insertion of tail-anchored proteins.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-10089316, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-10222271, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-10514571, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-10567422, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-10944333, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-11283351, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-12526792, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-12716905, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-14659697, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-15044454, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-15299926, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-16369096, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-16390866, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-16429126, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-16554755, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-16702403, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-16777091, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-17441508, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-17942943, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-18249086, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-18420932, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-18667436, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-18719252, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-18724936, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-18759457, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-19297527, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-19325107, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-19812306, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-8754838, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-9740675, http://linkedlifedata.com/resource/pubmed/commentcorrection/20106980-9757107
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, 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/HSP40 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Mdy2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Sgt2 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin, http://linkedlifedata.com/resource/pubmed/chemical/YDJ1 protein, S cerevisiae
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1083-351X
pubmed:author
pubmed:issnType
Electronic
pubmed:day
26
pubmed:volume
285
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9962-70
pubmed:dateRevised
2011-7-27
pubmed:meshHeading
pubmed-meshheading:20106980-Adenosine Triphosphatases, pubmed-meshheading:20106980-Carrier Proteins, pubmed-meshheading:20106980-Crystallography, X-Ray, pubmed-meshheading:20106980-Fungal Proteins, pubmed-meshheading:20106980-Gene Deletion, pubmed-meshheading:20106980-Gene Expression Profiling, pubmed-meshheading:20106980-Gene Expression Regulation, Fungal, pubmed-meshheading:20106980-Guanine Nucleotide Exchange Factors, pubmed-meshheading:20106980-HSP40 Heat-Shock Proteins, pubmed-meshheading:20106980-Mass Spectrometry, pubmed-meshheading:20106980-Molecular Chaperones, pubmed-meshheading:20106980-Protein Interaction Mapping, pubmed-meshheading:20106980-Protein Structure, Tertiary, pubmed-meshheading:20106980-Protein Transport, pubmed-meshheading:20106980-Saccharomyces cerevisiae, pubmed-meshheading:20106980-Saccharomyces cerevisiae Proteins, pubmed-meshheading:20106980-Two-Hybrid System Techniques, pubmed-meshheading:20106980-Ubiquitin
pubmed:year
2010
pubmed:articleTitle
Crystal structure of Get4-Get5 complex and its interactions with Sgt2, Get3, and Ydj1.
pubmed:affiliation
Institute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't