TY - JOUR
T1 - Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex
AU - Tripathi, Arati
AU - Ren, Yi
AU - Jeffrey, Philip D.
AU - Hughson, Frederick M.
N1 - Funding Information:
We gratefully acknowledge B. Kokona and R. Fairman for sedimentation velocity analytical ultracentrifugation; the staff of the National Synchrotron Light Source X25 and X29 beamlines for assistance with X-ray data collection; O. Perisic for advice on crystallization; M. Diefenbacher and A. Spang for many fruitful discussions and for communicating results before publication; K. Büssow (Max Planck Institute for Molecular Genetics, Berlin) for reagents; and S. Munro, M. Munson, A. Spang and members of the Hughson laboratory for critical comments on the manuscript. This work was supported by the US National Institutes of Health grant GM071574.
PY - 2009/2
Y1 - 2009/2
N2 - 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.
AB - 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.
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U2 - 10.1038/nsmb.1548
DO - 10.1038/nsmb.1548
M3 - Article
C2 - 19151722
AN - SCOPUS:59649120867
SN - 1545-9993
VL - 16
SP - 114
EP - 123
JO - Nature Structural and Molecular Biology
JF - Nature Structural and Molecular Biology
IS - 2
ER -