title: A role for the small GTPase Rab6 in assembly of human cytomegalovirus.
abstract: In human-cytomegalovirus (HCMV)-infected cells, the localization of the viral protein pp150 to the virus assembly compartment (AC) is dependent on its direct interaction with the cellular protein Bicaudal D1 through a dynein- and microtubule-dependent mechanism. We found that the small GTPase Rab6 also interacts indirectly with pp150 through its interaction with Bicaudal D1. Inhibition of Rab6 activity in HCMV-infected cells interrupted the intracellular trafficking of pp150, significantly reducing infectious virus production without affecting the formation of the AC, arguing for an important function for this cellular GTPase in the intracellular localization of pp150 during virus assembly.
authors.affiliation: Department of Pediatrics, School of Medicine, University of Alabama at Birmingham, Birmingham, Alabama, USA.
authors.forename: Sabarish V
authors.initials: SV
authors.lastname: Indran
authors.forename: William J
authors.initials: WJ
authors.lastname: Britt
mesh_terms: D002478:Cells, Cultured; D003587:Cytomegalovirus / Q000472:pathogenicity* / Q000502:physiology*; D005347:Fibroblasts / Q000821:virology; D054884:Host-Pathogen Interactions; D006801:Humans; D010750:Phosphoproteins / Q000378:metabolism*; D025941:Protein Interaction Mapping; D014763:Viral Matrix Proteins / Q000378:metabolism*; D019065:Virus Assembly; D020691:rab GTP-Binding Proteins / Q000378:metabolism*
chemical_list: D010750:Phosphoproteins; C094135:Rab6 protein; D014763:Viral Matrix Proteins; C056367:pp150 protein, Cytomegalovirus; D020691:rab GTP-Binding Proteins