期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 116, 期 48, 页码 24031-24040出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1909697116
关键词
membrane trafficking; COPI; vesicle coat; tethering complex; Dsl1
资金
- National Science Foundation (NSF) [MCB-1243656]
- National Institutes of Health (NIH) [T32GM007388, F31GM12676, R01GM071574]
- DOE Office of Science [DE-SC0012704]
- Life Science Biomedical Technology Research Resource - NIH, National Institute of General Medical Sciences (NIGMS) [P41GM111244]
- DOE Office of Biological and Environmental Research [KP1605010]
- NSF
- NIH/NIGMS under NSF [DMR-1332208]
- NIH, through its NIGMS [GM-103485]
Coat protein I (COPI)-coated vesicles mediate retrograde transport from the Golgi to the endoplasmic reticulum (ER), as well as transport within the Golgi. Major progress has been made in defining the structure of COPI coats, in vitro and in vivo, at resolutions as high as 9 angstrom. Nevertheless, important questions remain unanswered, including what specific interactions stabilize COPI coats, how COPI vesicles recognize their target membranes, and how coat disassembly is coordinated with vesicle fusion and cargo delivery. Here, we use X-ray crystallography to identify a conserved site on the COPI subunit alpha-COP that binds to flexible, acidic sequences containing a single tryptophan residue. One such sequence, found within alpha-COP itself, mediates alpha-COP homo-oligomerization. Another such sequence is contained within the lasso of the ER-resident Dsl1 complex, where it helps mediate the tethering of Golgi-derived COPI vesicles at the ER membrane. Together, our findings suggest that alpha-COP homo-oligomerization plays a key role in COPI coat stability, with potential implications for the coordination of vesicle tethering, uncoating, and fusion.
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