Structures and mechanisms of vesicle coat components and multisubunit tethering complexes.
Eukaryotic cells face a logistical challenge in ensuring prompt and precise delivery of vesicular cargo to specific organelles within the cell. Coat protein complexes select cargo and initiate vesicle formation, while multisubunit tethering complexes participate in the delivery of vesicles to target membranes. Understanding these macromolecular assemblies has greatly benefited from their structural characterization. Recent structural data highlight principles in coat recruitment and uncoating in both the endocytic and retrograde pathways, and studies on the architecture of tethering complexes provide a framework for how they might link vesicles to the respective acceptor compartments and the fusion machinery.
Cambridge Institute for Medical Research, Department of Clinical Biochemistry, University of Cambridge, Cambridge CB2 0XY, UK. lpj21@cam.ac.uk
Lauren P
LP
Jackson
Daniel
D
Kümmel
Karin M
KM
Reinisch
David J
DJ
Owen
D033942:Adaptor Proteins, Vesicular Transport / Q000378:metabolism; D034021:Auxilins / Q000378:metabolism; D001692:Biological Transport; D022181:COP-Coated Vesicles / Q000737:chemistry / Q000378:metabolism; D018699:Coated Vesicles / Q000737:chemistry* / Q000378:metabolism*; D006801:Humans; D021122:Protein Subunits / Q000737:chemistry* / Q000378:metabolism*
D033942:Adaptor Proteins, Vesicular Transport; D034021:Auxilins; D021122:Protein Subunits