A trapper keeper for TRAPP, its structures and functions.
During biosynthesis many membrane and secreted proteins are transported from the endoplasmic reticulum, through the Golgi and on to the plasma membrane in small transport vesicles. These transport vesicles have to undergo budding, movement, tethering, docking, and fusion at each organelle of the biosynthetic pathway. The transport protein particle (TRAPP) complex was initially identified as the tethering factor for endoplasmic reticulum (ER)-derived COPII vesicles, but the functions of TRAPP may extend to other areas of biology. Three forms of TRAPP complexes have been discovered to date, and recent advances in research have provided new insights on the structures and functions of TRAPP. Here we provide a comprehensive review of the recent findings in TRAPP biology.
School of Biomedical Sciences and Epithelial Cell Biology Research Center, The Chinese University of Hong Kong, Shatin, N.T., Hong Kong SAR, People's Republic of China, sidney.yu@cuhk.edu.hk.
Sidney
S
Yu
Yongheng
Y
Liang
D000818:Animals; D022181:COP-Coated Vesicles / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D011485:Protein Binding; D021381:Protein Transport; D033921:Vesicular Transport Proteins / Q000378:metabolism*
D033921:Vesicular Transport Proteins; C406327:transport protein particle, TRAPP