Compton Shannon L, Behrend Ellen N
Department of Biomedical Science, Auburn University, Auburn, AL, USA.
Biochem Cell Biol. 2006 Dec;84(6):940-8. doi: 10.1139/o06-176.
Prenylated Rab acceptor domain family member 1 (PRAF1), a transmembrane protein whose precise function is unknown, localizes to the Golgi complex, post-Golgi vesicles, lipid rafts, endosomes, and the plasma membrane. VAMP2 and Rab3A are SNARE proteins that interact with PRAF1, and, as part of a SNARE complex, PRAF1 may function in the regulation of docking and fusion of transport vesicles both in the Golgi complex and at the plasma membrane. Alternately, PRAF1 may function as a sorting protein in the Golgi complex. In addition to interacting with SNARE proteins, PRAF1 interacts with rotaviral, retroviral, and herpes viral proteins. The function of viral protein interaction is unknown, but PRAF1 may enhance rotaviral and retroviral assembly. In contrast, PRAF1 may inhibit the herpes virus life cycle.
异戊二烯化Rab受体结构域家族成员1(PRAF1)是一种跨膜蛋白,其确切功能尚不清楚,定位于高尔基体复合体、高尔基体后囊泡、脂筏、内体和质膜。VAMP2和Rab3A是与PRAF1相互作用的可溶性N-乙基马来酰胺敏感因子附着蛋白受体(SNARE)蛋白,作为SNARE复合体的一部分,PRAF1可能在高尔基体复合体和质膜中运输囊泡的对接和融合调控中发挥作用。另外,PRAF1可能在高尔基体复合体中作为一种分选蛋白发挥作用。除了与SNARE蛋白相互作用外,PRAF1还与轮状病毒、逆转录病毒和疱疹病毒蛋白相互作用。病毒蛋白相互作用的功能尚不清楚,但PRAF1可能会增强轮状病毒和逆转录病毒的组装。相反,PRAF1可能会抑制疱疹病毒的生命周期。