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- W2116964023 abstract "The Dsl1p tethering complex is crucial for Golgi-to-ER retrograde trafficking of vesicles in yeast. The crystal structures of two out of three Dsl1p complex components reveal similarity to exocyst and COG complex components, which act in tethering vesicles to the plasma membrane and Golgi, respectively, suggesting a conserved tethering strategy at several eukaryotic membranes. 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 α-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." @default.
- W2116964023 created "2016-06-24" @default.
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- W2116964023 date "2009-01-18" @default.
- W2116964023 modified "2023-10-17" @default.
- W2116964023 title "Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex" @default.
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- W2116964023 doi "https://doi.org/10.1038/nsmb.1548" @default.
- W2116964023 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2635920" @default.
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