Identification and molecular interacting network of the conserved oligomeric Golgi (COG) tethering complex

Abstract

Protein transport along the secretory and endocytic pathway is mediated by vesicular carriers which bud from one compartment, then target and fuse with their correct destination in the pathway. This highly regulated process involves the combination of various classes of proteins, amongst which are tethers and SNAREs. We have characterized mammalian Sec34/Cog3, important for endoplasmic reticulum-to-Golgi transport and have shown that it is a part of an 8-subunit COG complex. We have also proposed a model for the assembly of this complex. In addition, results of studies done on two other proteins- mammalian Bet3 (which is one of the subunits of the TRAPP complex) and syntaxin 8 (a SNARE protein) are also presented.