GET3/YDL100C Literature Guide Help

Other names published for GET3: ARR4, guanine nucleotide exchange factor GET3, YDL100C

GET3 - Strains/Constructs (28)

ReferenceOther Genes Addressed
Chang YW, et al.  (2012) Interaction surface and topology of Get3-Get4-Get5 protein complex, involved in targeting tail-anchored proteins to endoplasmic reticulum. J Biol Chem 287(7):4783-9
Hodgins-Davis A, et al.  (2012) Abundant gene-by-environment interactions in gene expression reaction norms to copper within Saccharomyces cerevisiae. Genome Biol Evol 4(11):1061-79
Katrin K, et al.  (2012) Ergosterol content specifies targeting of tail-anchored proteins to mitochondrial outer membranes. Mol Biol Cell 23(20):3927-35
Boettner DR, et al.  (2011) Clathrin light chain directs endocytosis by influencing the binding of the yeast Hip1R homologue, Sla2, to F-actin. Mol Biol Cell 22(19):3699-714
Mariappan M, et al.  (2011) The mechanism of membrane-associated steps in tail-anchored protein insertion. Nature 477(7362):61-6
Stefer S, et al.  (2011) Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex. Science 333(6043):758-62
Wang F, et al.  (2011) The mechanism of tail-anchored protein insertion into the ER membrane. Mol Cell 43(5):738-50
Leznicki P, et al.  (2010) Bat3 promotes the membrane integration of tail-anchored proteins. J Cell Sci 123(Pt 13):2170-8
Tani A, et al.  (2010) Genes involved in novel adaptive aluminum resistance in Rhodotorula glutinis. J Biosci Bioeng 109(5):453-8
Wang F, et al.  (2010) A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol Cell 40(1):159-71
Yamagata A, et al.  (2010) Structural insight into the membrane insertion of tail-anchored proteins by Get3. Genes Cells 15(1):29-41
Garbarino J, et al.  (2009) Sterol and diacylglycerol acyltransferase deficiency triggers fatty acid-mediated cell death. J Biol Chem 284(45):30994-1005
Jonikas MC, et al.  (2009) Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323(5922):1693-7
Mateja A, et al.  (2009) The structural basis of tail-anchored membrane protein recognition by Get3. Nature 461(7262):361-6
Metzger MB and Michaelis S  (2009) Analysis of quality control substrates in distinct cellular compartments reveals a unique role for Rpn4p in tolerating misfolded membrane proteins. Mol Biol Cell 20(3):1006-19
Suloway CJ, et al.  (2009) Model for eukaryotic tail-anchored protein binding based on the structure of Get3. Proc Natl Acad Sci U S A 106(35):14849-54
Lee MJ and Dohlman HG  (2008) Coactivation of G protein signaling by cell-surface receptors and an intracellular exchange factor. Curr Biol 18(3):211-5
Ruotolo R, et al.  (2008) Membrane transporters and protein traffic networks differentially affecting metal tolerance: a genomic phenotyping study in yeast. Genome Biol 9(4):R67
Schuldiner M, et al.  (2008) The GET complex mediates insertion of tail-anchored proteins into the ER membrane. Cell 134(4):634-45
Zakrzewska A, et al.  (2007) Cellular Processes and Pathways That Protect Saccharomyces cerevisiae Cells against the Plasma Membrane-Perturbing Compound Chitosan. Eukaryot Cell 6(4):600-8
Auld KL, et al.  (2006) The Conserved ATPase Get3/Arr4 Modulates the Activity of Membrane-Associated Proteins in Saccharomyces cerevisiae. Genetics 174(1):215-27
Metz J, et al.  (2006) The yeast Arr4p ATPase binds the chloride transporter Gef1p when copper is available in the cytosol. J Biol Chem 281(1):410-7
Schuldiner M, et al.  (2005) Exploration of the function and organization of the yeast early secretory pathway through an epistatic miniarray profile. Cell 123(3):507-19
Tong AH, et al.  (2004) Global mapping of the yeast genetic interaction network. Science 303(5659):808-13
Huh WK, et al.  (2003) Global analysis of protein localization in budding yeast. Nature 425(6959):686-91
Shen J, et al.  (2003) The Saccharomyces cerevisiae Arr4p is involved in metal and heat tolerance. Biometals 16(3):369-78
de Groot PW, et al.  (2001) A genomic approach for the identification and classification of genes involved in cell wall formation and its regulation in Saccharomyces cerevisiae. Comp Funct Genomics 2(3):124-42
Zuniga S, et al.  (1999) Disruption of six Saccharomyces cerevisiae novel genes and phenotypic analysis of the deletants. Yeast 15(10B):945-53