3etu
Crystal structure of yeast Dsl1pCrystal structure of yeast Dsl1p
Structural highlights
FunctionDSL1_YEAST Required for protein transport between the Golgi and the endoplasmic reticulum. May tether coatomer-coated retrograde transport vesicles to the ER membrane through interaction with coatomer as well as the SNARE complex. May contribute to the stabilization of the SNARE complex.[1] [2] [3] Publication Abstract from PubMedMultisubunit 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. Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex.,Tripathi A, Ren Y, Jeffrey PD, Hughson FM Nat Struct Mol Biol. 2009 Feb;16(2):114-23. Epub 2009 Jan 18. PMID:19151722[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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