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TitleMolecular architecture of the TRAPPII complex and implications for vesicle tethering.
Journal, issue, pagesNat Struct Mol Biol, Vol. 17, Issue 11, Page 1298-1304, Year 2010
Publish dateOct 24, 2010
AuthorsCalvin K Yip / Julia Berscheminski / Thomas Walz /
PubMed AbstractMultisubunit tethering complexes participate in the process of vesicle tethering--the initial interaction between transport vesicles and their acceptor compartments. TRAPPII (named for transport ...Multisubunit tethering complexes participate in the process of vesicle tethering--the initial interaction between transport vesicles and their acceptor compartments. TRAPPII (named for transport protein particle II) is a highly conserved tethering complex that functions in the late Golgi apparatus and consists of all of the subunits of TRAPPI and three additional, specific subunits. We have purified native yeast TRAPPII and characterized its structure and subunit organization by single-particle EM. Our data show that the nine TRAPPII components form a core complex that dimerizes into a three-layered, diamond-shaped structure. The TRAPPI subunits assemble into TRAPPI complexes that form the outer layers. The three TRAPPII-specific subunits cap the ends of TRAPPI and form the middle layer, which is responsible for dimerization. TRAPPII binds the Ypt1 GTPase and probably uses the TRAPPI catalytic core to promote guanine nucleotide exchange. We discuss the implications of the structure of TRAPPII for coat interaction and TRAPPII-associated human pathologies.
External linksNat Struct Mol Biol / PubMed:20972447 / PubMed Central
MethodsEM (single particle)
Resolution32.0 - 34.0 Å
Structure data

EMDB-5213:
Molecular architecture of the yeast TRAPPII tethering complex - form1
Method: EM (single particle) / Resolution: 32.0 Å

EMDB-5214:
Molecular architecture of the yeast TRAPPII tethering complex - form2
Method: EM (single particle) / Resolution: 34.0 Å

Source
  • Saccharomyces cerevisiae (brewer's yeast)

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