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Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex.

Nature structural & molecular biology | 2009

Multisubunit tethering complexes are essential for intracellular trafficking and have been proposed to mediate the initial interaction between vesicles and the membranes with which they fuse. Here we report initial structural characterization of the Dsl1p complex, whose three subunits are essential for trafficking from the Golgi apparatus to the endoplasmic reticulum (ER). Crystal structures reveal that two of the three subunits, Tip20p and Dsl1p, resemble known subunits of the exocyst complex, establishing a structural connection among several multisubunit tethering complexes and implying that many of their subunits are derived from a common progenitor. We show, moreover, that Tip20p and Dsl1p interact directly via N-terminal alpha-helices. Finally, we establish that different Dsl1p complex subunits bind independently to different ER SNARE proteins. Our results map out two alternative protein-interaction networks capable of tethering COPI-coated vesicles, via the Dsl1p complex, to ER membranes.

Pubmed ID: 19151722 RIS Download

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Associated grants

  • Agency: NIBIB NIH HHS, United States
    Id: P30 EB009998
  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM071574
  • Agency: NIGMS NIH HHS, United States
    Id: R01 GM071574-05
  • Agency: NIGMS NIH HHS, United States
    Id: GM071574

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