Structural characterization of the Get4/Get5 complex and its interaction with Get3

The recently elucidated Get proteins are responsible for the targeted delivery of the majority of tail-anchored (TA) proteins to the endoplasmic reticulum. Get4 and Get5 have been identified in the early steps of the pathway mediating TA substrate delivery to the cytoplasmic targeting factor Get3. H...

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Veröffentlicht in:	Proceedings of the National Academy of Sciences - PNAS 2010-07, Vol.107 (27), p.12127-12132
Hauptverfasser:	Chartron, Justin W., Suloway, Christian J. M., Zaslaver, Ma'ayan, Clemons, William M., Rees, Douglas C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Binding Sites Biochemistry Biological Sciences Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Crystal structure Crystallography, X-Ray Cytoplasm Dimerization Dimers Escherichia coli - genetics Genetic Complementation Test Guanine Nucleotide Exchange Factors - chemistry Guanine Nucleotide Exchange Factors - genetics Guanine Nucleotide Exchange Factors - metabolism Membrane Proteins Models, Molecular Monomers Mutation Nucleotides Phenotypes Protein Binding Protein Interaction Mapping Protein Structure, Tertiary Proteins Recombinant Proteins - chemistry Recombinant Proteins - metabolism Ribosomes Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - growth & development Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Substrate Specificity Ubiquitin - chemistry Ubiquitin - genetics Ubiquitin - metabolism Yeast Yeasts
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