Affiliation: University of Cambridge
- ER-to-Golgi transport: COP I and COP II function (Review)Rainer Duden
Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Hills Road, Cambridge CB2 2XY, UK
Mol Membr Biol 20:197-207. 2003..Additionally, COP I coat proteins have complex functions in intra-Golgi trafficking and in maintaining the normal structure of the mammalian interphase Golgi complex...
- Molecular basis for recognition of dilysine trafficking motifs by COPILauren P Jackson
Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Hills Road, Cambridge CB2 0XY, UK
Dev Cell 23:1255-62. 2012..Flexibility between β'-COP WD-repeat domains and the location of cargo binding have implications for COPI coat assembly...
- Two human ARFGAPs associated with COP-I-coated vesiclesGabriella Frigerio
Department of Clinical Biochemistry, Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge CB2 2XY, United Kingdom
Traffic 8:1644-55. 2007..However, silencing all three ARFGAPs causes cell death. Our data provide strong evidence that ARFGAP2 and ARFGAP3 function in COP I traffic...
- The alpha- and beta'-COP WD40 domains mediate cargo-selective interactions with distinct di-lysine motifsAnne Eugster
Department of Clinical Biochemistry, Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, United Kingdom
Mol Biol Cell 15:1011-23. 2004....
- Gamma-COP appendage domain - structure and functionPeter J Watson
Cambridge Institute for Medical Research and Department of Clinical Biochemistry, University of Cambridge, Hills Road, Cambridge CB2 2XY, UK
Traffic 5:79-88. 2004..On the basis of mutations in the yeast homologue of gamma-COP, Sec21p, a second binding site is proposed to exist on the gamma-COP appendage that interacts with the alpha,beta',epsilon COPI subcomplex...
- Peptide-receptive major histocompatibility complex class I molecules cycle between endoplasmic reticulum and cis-Golgi in wild-type lymphocytesMalgorzata Garstka
Biochemistry and Cell Biology, School of Engineering and Science, Jacobs University Bremen, 28759 Bremen, Germany
J Biol Chem 282:30680-90. 2007....
- ArfGAP1 dynamics and its role in COPI coat assembly on Golgi membranes of living cellsWei Liu
Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA
J Cell Biol 168:1053-63. 2005..These data suggest that ArfGAP1, coatomer and Arf1 play interdependent roles in the assembly-disassembly cycle of the COPI coat in vivo...
- The Sec34/Sec35p complex, a Ypt1p effector required for retrograde intra-Golgi trafficking, interacts with Golgi SNAREs and COPI vesicle coat proteinsElena S Suvorova
Department of Physiology and Biophysics, University of Arkansas for Medical Sciences, Little Rock, AR 72205, USA
J Cell Biol 157:631-43. 2002..We propose that the Sec34/35 protein complex acts as a tether that connects cis-Golgi membranes and COPI-coated, retrogradely targeted intra-Golgi vesicles...
- 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...
- Vesicular trafficking: 7th Young Scientists meeting of the German Society for Cell Biology (DGZ) - Jena, September 22nd to 24th, 2005Rainer Duden
School of Biological Sciences, Royal Holloway, University of London, Egham, Surrey TW20 0EX, UK
Eur J Cell Biol 85:133-40. 2006
- Crn7 interacts with AP-1 and is required for the maintenance of Golgi morphology and protein export from the GolgiVasily Rybakin
Institute for Biochemistry I, Medical Faculty, University of Cologne, Joseph Stelzmann Strasse 52, D 50931 Cologne, Germany
J Biol Chem 281:31070-8. 2006..We identify tyrosine 288-based motif as part of a canonical YXXPhi sorting signal and a major mu1-adaptin binding site in vitro. This study provides the first insight into the function of mammalian Crn7 protein in the Golgi complex...