PRAF1: a Golgi complex transmembrane protein that interacts with viruses

• Published in: Biochemistry and cell biology Vol. 84; no. 6; pp. 940 - 948
• Main Authors: Compton, Shannon L, Behrend, Ellen N
• Format: Journal Article
• Language: English
• Published: Canada NRC Research Press 01.12.2006
• Subjects: Animals; CHO Cells; Control; Cricetinae; Cricetulus; Golgi apparatus; Golgi Apparatus - genetics; Golgi Apparatus - metabolism; GTP-Binding Proteins - genetics; GTP-Binding Proteins - metabolism; Humans; Membrane proteins; Membrane Proteins - genetics; Membrane Proteins - metabolism; Properties; Protein Prenylation; Protein-protein interactions; Vesicular Transport Proteins - genetics; Vesicular Transport Proteins - metabolism; Viral proteins; Viruses - metabolism; United States
• ISSN: 0829-8211; 1208-6002
• 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.