MDY2/YOL111C Literature Guide Help

Other names published for MDY2: TMA24, GET5, YOL111C

MDY2 - Primary Literature (21)

ReferenceOther Genes Addressed
Ast T, et al.  (2013) A network of cytosolic factors targets SRP-independent proteins to the endoplasmic reticulum. Cell 152(5):1134-45
Leznicki P, et al.  (2013) The Association of BAG6 with SGTA and Tail-Anchored Proteins. PLoS One 8(3):e59590
Simon AC, et al.  (2013) Structure of the Sgt2/Get5 complex provides insights into GET-mediated targeting of tail-anchored membrane proteins. Proc Natl Acad Sci U S A 110(4):1327-32
Arhzaouy K and Ramezani-Rad M  (2012) Nuclear Import of UBL-Domain Protein Mdy2 Is Required for Heat-Induced Stress Response in Saccharomyces cerevisiae. PLoS One 7(12):e52956
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
Chartron JW, et al.  (2012) Get5 carboxyl-terminal domain is a novel dimerization motif that tethers an extended Get4/Get5 complex. J Biol Chem 287(11):8310-7
Chartron JW, et al.  (2012) Structures of the Sgt2/SGTA dimerization domain with the Get5/UBL4A UBL domain reveal an interaction that forms a conserved dynamic interface. Cell Rep 2(6):1620-32
Kiktev DA, et al.  (2012) Regulation of chaperone effects on a yeast prion by cochaperone Sgt2. Mol Cell Biol 32(24):4960-70
Chartron JW, et al.  (2011) A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex. J Biol Chem 286(39):34325-34
Kohl C, et al.  (2011) Cooperative and independent activities of Sgt2 and Get5 in the targeting of tail-anchored proteins. Biol Chem 392(7):601-8
Chang YW, et al.  (2010) Crystal structure of Get4-Get5 complex and its interactions with Sgt2, Get3, and Ydj1. J Biol Chem 285(13):9962-70
Chartron JW, et al.  (2010) Structural characterization of the Get4/Get5 complex and its interaction with Get3. Proc Natl Acad Sci U S A 107(27):12127-32
Cohnen A, et al.  (2010) The yeast ubiquitin-like domain protein Mdy2 is required for microtubule-directed nuclear migration and localizes to cytoplasmic granules in response to heat stress. Cytoskeleton (Hoboken) 67(10):635-49
Leznicki P, et al.  (2010) Bat3 promotes the membrane integration of tail-anchored proteins. J Cell Sci 123(Pt 13):2170-8
Wang F, et al.  (2010) A chaperone cascade sorts proteins for posttranslational membrane insertion into the endoplasmic reticulum. Mol Cell 40(1):159-71
Copic A, et al.  (2009) Genomewide analysis reveals novel pathways affecting endoplasmic reticulum homeostasis, protein modification and quality control. Genetics 182(3):757-69
Jonikas MC, et al.  (2009) Comprehensive characterization of genes required for protein folding in the endoplasmic reticulum. Science 323(5922):1693-7
Liou ST, et al.  (2007) SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae. Cell Stress Chaperones 12(1):59-70
Fleischer TC, et al.  (2006) Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes. Genes Dev 20(10):1294-307
Hu Z, et al.  (2006) Mdy2, a ubiquitin-like (UBL)-domain protein, is required for efficient mating in Saccharomyces cerevisiae. J Cell Sci 119(Pt 2):326-38
Iwanejko L, et al.  (1999) Disruption and functional analysis of six ORFs on chromosome XV: YOL117w, YOL115w ( TRF4), YOL114c, YOL112w ( MSB4), YOL111c and YOL072w. Yeast 15(14):1529-39