Genomes and Genes
Gene Symbol: RET2
Species: Saccharomyces cerevisiae S288c
- Architecture of coatomer: molecular characterization of delta-COP and protein interactions within the complexD Faulstich
Institut fur Biochemie I, Heidelberg, Germany
J Cell Biol 135:53-61. 1996..We propose that these interactions reflect in vivo associations of those subunits and thus play a functional role in the assembly of coatomer and/or serve to maintain the molecular architecture of the complex...
- Golgi-to-endoplasmic reticulum (ER) retrograde traffic in yeast requires Dsl1p, a component of the ER target site that interacts with a COPI coat subunitB A Reilly
Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA
Mol Biol Cell 12:3783-96. 2001..Last, we show that Dsl1p interacts with the delta-subunit of the retrograde COPI coat, Ret2p, and discuss possible roles for this interaction...
- COP I domains required for coatomer integrity, and novel interactions with ARF and ARF-GAPA Eugster
Department of Clinical Biochemistry, University of Cambridge, Hills Road, Cambridge CB2 2XY, UK
EMBO J 19:3905-17. 2000..Glo3p also interacts with intact coatomer in vitro...
- Isoform-selective oligomer formation of Saccharomyces cerevisiae p24 family proteinsRyogo Hirata
From the Live Cell Molecular Imaging Research Team, RIKEN Center for Advanced Photonics and
J Biol Chem 288:37057-70. 2013..This complex was mainly localized to the Golgi, whereas the p24 complex containing Erv25, instead of Rrt6 but otherwise with the same isoform composition, was found mostly in the ER. ..
- Molecular structure and flexibility of the yeast coatomer as revealed by electron microscopyCalvin K Yip
Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA
J Mol Biol 408:825-31. 2011..Our analyses provide the first three-dimensional picture of the complete coatomer and reveal substantial conformational flexibility likely to be critical for its scaffolding function...
- Sgf1p, a new component of the Sec34p/Sec35p complexD W Kim
Department of Cell Biology and Howard Hughes Medical Institute, Yale University, New Haven, CT, USA
Traffic 2:820-30. 2001..Although an earlier study suggested that Sec34p (Grd20p) is not required for protein secretion, we show here that the sec34-2 and sec35-1 mutations lead to a pleiotropic block in the secretion of all proteins into the growth medium...
- A structure-based mechanism for Arf1-dependent recruitment of coatomer to membranesXinchao Yu
Howard Hughes Medical Institute and the Structural Biology Program, Memorial Sloan Kettering Cancer Center, 1275 York Avenue, New York, NY 10065, USA
Cell 148:530-42. 2012..A bivalent GTP-dependent binding mode has implications for the dynamics of coatomer interaction with the Golgi and for the selection of cargo molecules...
- Rsp5 ubiquitin ligase is required for protein trafficking in Saccharomyces cerevisiae COPI mutantsKatarzyna Jarmoszewicz
Department of Genetics, Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland
PLoS ONE 7:e39582. 2012..Additionally, Rsp5 and Sla1 proteins were found by co-immunoprecipitation in a complex containing COPI subunits. Together, our results show that Rsp5 ligase plays a role in regulating retrograde Golgi-to-ER trafficking...
- Signal-mediated dynamic retention of glycosyltransferases in the GolgiLinna Tu
Department of Biology, Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong, Special Administrative Region SAR of the People s Republic of China
Science 321:404-7. 2008..We propose that Vps74p maintains the steady-state localization of Golgi glycosyltransferases dynamically, by promoting their incorporation into COPI-coated vesicles...
- Ypt11 functions in bud-directed transport of the Golgi by linking Myo2 to the coatomer subunit Ret2Seisuke Arai
Department of Biotechnology, University of Tokyo, Yayoi, Bunkyo ku, Tokyo 113 8657, Japan
Curr Biol 18:987-91. 2008..Here, we report that Ypt11, a Rab GTPase that reportedly interacts with Myo2, binds to Ret2, a subunit of the coatomer complex...
- Novel cargo-binding site in the beta and delta subunits of coatomerKai Michelsen
Zentrum fur Molekulare Biologie der Universitat Heidelberg, Im Neuenheimer Feld 282, D 69120 Heidelberg, Germany
J Cell Biol 179:209-17. 2007..A homology model of the COPI trunk domain illustrates the recognition of R-based signals by COPI...
- Dsl1p, an essential component of the Golgi-endoplasmic reticulum retrieval system in yeast, uses the same sequence motif to interact with different subunits of the COPI vesicle coatUwe Andag
Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, D 37070 Goettingen, Germany
J Biol Chem 278:51722-34. 2003..They interact with different layers of the vesicle coat by using tandemly arranged sequence motifs, some of which have dual specificity...
- ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coatUlrike Rein
Friedrich Miescher Laboratory, Max Planck Society, D 72076 Tubingen, Germany
J Cell Biol 157:395-404. 2002..The mechanisms by which v-SNAREs interact with COPI and COPII coat proteins seem to be different and may play a key role in determining specificity in vesicle budding...
- The Saccharomyces cerevisiae early secretion mutant tip20 is synthetic lethal with mutants in yeast coatomer and the SNARE proteins Sec22p and Ufe1pG Frigerio
Sanger Centre, Wellcome Trust Genome Campus, Hinxton, Cambridge, UK
Yeast 14:633-46. 1998..temperature-sensitive tip20 mutants are shown to be lethal in combination with ufe1-1, a target SNARE of the ER and ret2-1, yeast delta-COP...
- Delta- and zeta-COP, two coatomer subunits homologous to clathrin-associated proteins, are involved in ER retrievalP Cosson
Basel Institute for Immunology, Switzerland
EMBO J 15:1792-8. 1996..While both ret2-1 and ret3-1 were defective for ER retrieval, only ret2-1 exhibited a defect in forward ER-to-Golgi transport at ..
- Alpha-COP can discriminate between distinct, functional di-lysine signals in vitro and regulates access into retrograde transportS Schröder-Köhne
Max Planck Institut fur biophysikalische Chemie, D 37070 Gottingen, Germany
J Cell Sci 111:3459-70. 1998..Therefore, the retrograde transport of Emp47p displayed a differential requirement for individual coatomer subunits and a special role of alpha-COP for a particular transport step in vivo...