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RISS 인기검색어
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- 저자 : Munger, Christine (검색결과 2 건)
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The Architecture of the Multisubunit TRAPP I Complex Suggests a Model for Vesicle Tethering
Kim, Yeon-Gil,Raunser, Stefan,Munger, Christine,Wagner, John,Song, Young-Lan,Cygler, Miroslaw,Walz, Thomas,Oh, Byung-Ha,Sacher, Michael Elsevier 2006 Cell Vol.127 No.4
<P><B>Summary</B></P><P>Transport protein particle (TRAPP) I is a multisubunit vesicle tethering factor composed of seven subunits involved in ER-to-Golgi trafficking. The functional mechanism of the complex and how the subunits interact to form a functional unit are unknown. Here, we have used a multidisciplinary approach that includes X-ray crystallography, electron microscopy, biochemistry, and yeast genetics to elucidate the architecture of TRAPP I. The complex is organized through lateral juxtaposition of the subunits into a flat and elongated particle. We have also localized the site of guanine nucleotide exchange activity to a highly conserved surface encompassing several subunits. We propose that TRAPP I attaches to Golgi membranes with its large flat surface containing many highly conserved residues and forms a platform for protein-protein interactions. This study provides the most comprehensive view of a multisubunit vesicle tethering complex to date, based on which a model for the function of this complex, involving Rab1-GTP and long, coiled-coil tethers, is presented.</P>
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Kim, Min‐,Sung,Yi, Min‐,Ju,Lee, Kwang‐,Hoon,Wagner, John,Munger, Christine,Kim, Yeon‐,Gil,Whiteway, Malcolm,Cygler, Miroslaw,Oh, Byung‐,Ha,Sacher, Michael Blackwell Publishing Ltd 2005 Traffic Vol.6 No.12
<P><B>Transport protein particle (TRAPP) comprises a family of two highly related multiprotein complexes, with seven common subunits, that serve to target different classes of transport vesicles to their appropriate compartments. Defining the architecture of the complexes will advance our understanding of the functional differences between these highly related molecular machines. Genetic analyses in yeast suggested a specific interaction between the TRAPP subunits Bet3p and Trs33p. A mammalian bet3–trs33 complex was crystallized, and the structure was solved to 2.2 Å resolution. Intriguingly, the overall fold of the bet3 and trs33 monomers was similar, although the proteins had little overall sequence identity. <I>In vitro</I> experiments using yeast TRAPP subunits indicated that Bet3p binding to Trs33p facilitates the interaction between Bet3p and another TRAPP subunit, Bet5p. Mutational analysis suggests that yeast Trs33p facilitates other Bet3p protein–protein interactions. Furthermore, we show that Trs33p can increase the Golgi‐localized pool of a mutated Bet3 protein normally found in the cytosol. We propose that one of the roles of Trs33p is to facilitate the incorporation of the Bet3p subunit into assembling TRAPP complexes.</B></P>
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