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PDBsum entry 3etu
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Transport protein
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PDB id
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3etu
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References listed in PDB file
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Key reference
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Title
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Structural characterization of tip20p and dsl1p, Subunits of the dsl1p vesicle tethering complex.
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Authors
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A.Tripathi,
Y.Ren,
P.D.Jeffrey,
F.M.Hughson.
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Ref.
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Nat Struct Biol, 2009,
16,
114-123.
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PubMed id
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Abstract
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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.
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