Structure and mechanism of COPI vesicle biogenesis.
Distinct trafficking pathways within the secretory and endocytic systems ensure prompt and precise delivery of specific cargo molecules to different cellular compartments via small vesicular (50-150nm) and tubular carriers. The COPI vesicular coat is required for retrograde trafficking from the cis-Golgi back to the ER and within the Golgi stack. Recent structural data have been obtained from X-ray crystallographic studies on COPI coat components alone and on COPI subunits in complex with either cargo motifs or Arf1, and from reconstructions of COPI coated vesicles by electron tomography. These studies provide important molecular information and indicate key differences in COPI coat assembly as compared with clathrin-based and COPII-based coats.
Department of Biological Sciences, Vanderbilt University, Nashville, TN 37235, USA. Electronic address: lauren.p.jackson@vanderbilt.edu.
Lauren P
LP
Jackson
D000818:Animals; D001692:Biological Transport; D022181:COP-Coated Vesicles / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D020755:Coat Protein Complex I / Q000378:metabolism*; D004151:Dipeptides / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006801:Humans; D011485:Protein Binding
D020755:Coat Protein Complex I; D004151:Dipeptides; D006160:Guanosine Triphosphate; C024575:lysyllysine