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Journal home Advance online publication Current issue Archive Press releases Supplements Focus Guide to authors Online submission Permissions For referees Free online issue Contact the journal Subscribe Advertising work@npg naturereprints About this site For librarians   NPG Resources Nature Nature Cell Biology Nature Reviews Molecular Cell Biology The EMBO Journal Nature Reports Avian Flu NPG Subject areas Biotechnology Cancer Chemistry Clinical Medicine Dentistry Development Drug Discovery Earth Sciences Evolution & Ecology Genetics Immunology Materials Science Medical Research Microbiology Molecular Cell Biology Neuroscience Pharmacology Physics Browse all publications Article Nature Structural & Molecular Biology  12, 38 - 45 (2004) Published online: 19 December 2004; | doi:10.1038/nsmb871 Crystal structure of bet3 reveals a novel mechanism for Golgi localization of tethering factor TRAPP Yeon-Gil Kim1, Eun Ju Sohn2, Jawon Seo3, Kong-Joo Lee3, Heung-Soo Lee4, Inhwan Hwang2, Malcolm Whiteway5, Michael Sacher6 & Byung-Ha Oh1 1  Center for Biomolecular Recognition, Department of Life Science and Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang, Kyungbuk, 790-784, Korea. 2  Center for Plant Intracellular Trafficking, Department of Life Science and Division of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang, Kyungbuk, 790-784, Korea. 3  Center for Cell Signaling Research, Division of Molecular Life Sciences and College of Pharmacy, Ewha Womans University, Seoul, 120-750, Korea. 4  Pohang Accelerator Laboratory, Pohang, Kyungbuk, 790-784, Korea. 5  Biotechnology Research Institute, 6100 Royalmount Avenue, Montreal, Quebec, Canada H4P 2R2. 6  Montreal Proteomics Network, 6100 Royalmount Avenue, Montreal, Quebec, Canada H4P 2R2. Correspondence should be addressed to Byung-Ha Oh bhoh@postech.ac.kr or Michael Sacher michael.sacher@bri.nrc.caTransport protein particle (TRAPP) is a large multiprotein complex involved in endoplasmic reticulum−to−Golgi and intra-Golgi traffic. TRAPP specifically and persistently resides on Golgi membranes. Neither the mechanism of the subcellular localization nor the function of any of the individual TRAPP components is known. Here, the crystal structure of mouse Bet3p (bet3), a conserved TRAPP component, reveals a dimeric structure with hydrophobic channels. The channel entrances are located on a putative membrane-interacting surface that is distinctively flat, wide and decorated with positively charged residues. Charge-inversion mutations on the flat surface of the highly conserved yeast Bet3p led to conditional lethality, incorrect localization and membrane trafficking defects. A channel-blocking mutation led to similar defects. These data delineate a molecular mechanism of Golgi-specific targeting and anchoring of Bet3p involving the charged surface and insertion of a Golgi-specific hydrophobic moiety into the channels. This essential subunit could then direct other TRAPP components to the Golgi. MORE ARTICLES LIKE THIS These links to content published by NPG are automatically generated. NEWS AND VIEWS Sticky fingers and CAAX boxes Nature News and Views (08 Sep 1988) RESEARCH How curved membranes recruit amphipathic helices and protein anchoring motifs Nature Chemical Biology Article (01 Nov 2009) Structure of palmitoylated BET3: insights into TRAPP complex assembly and membrane localization The EMBO Journal Article (09 Mar 2005) See all 27 matches for Research  Top Abstract Previous | Next Table of contents Full text Download PDF Send to a friend Save this link Open Innovation Challenges Direct Molecular Detection of Proteins and Nucleic Acids Deadline: Dec 02 2009 Reward: $5,000 USD This Challenge is looking for novel approaches to protein and nucleic acid detection. This is an Id... Methods of Modeling Adaptation in Populations Deadline: Dec 30 2009 Reward: $15,000 USD The analysis of adaptation with a population is a frequently encountered computational modeling scen... More Challenges Powered by: nature jobs Admission for Research Scholars Program CDFD (Centre for DNA Fingerprinting and Diagnostics) Hyderabad, A.P. 500 001 India Senior Position: Evolutionary Microbial Pathogenesis Michigan State University (MSU), Dept. of Microbiology & Molecular Genetics 2215 Biomedical & Physical Sciences, East Lansing, MI 48824 More science jobs Post a job for free Figures & Tables Supplementary info Export citation Search buyers guide:   ADVERTISEMENT

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