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• W2032067173 abstract "The envelope of human cytomegalovirus (HCMV) consists of a large number of glycoproteins. The most abundant glycoprotein in the HCMV envelope is the glycoprotein M (UL100), which together with glycoprotein N (UL73) form the gM/gN protein complex. Using yeast two-hybrid screening, we found that the gM carboxy-terminal cytoplasmic tail (gM-CT) interacts with FIP4, a Rab11-GTPase effector protein. Depletion of FIP4 expression in HCMV-infected cells resulted in a decrease in infectious virus production that was also associated with an alteration of the HCMV assembly compartment (AC) phenotype. A similar phenotype was also observed in HCMV-infected cells that expressed dominant negative Rab11(S25N). Recently, it has been shown that FIP4 interactions with Rab11 and additionally with Arf6/Arf5 are important for the vesicular transport of proteins in the endosomal recycling compartment (ERC) and during cytokinesis. Surprisingly, FIP4 interaction with gM-CT limited binding of FIP4 with Arf5/Arf6; however, FIP4 interaction with gM-CT did not prevent recruitment of Rab11 into the ternary complex. These data argued for a contribution of the ERC during cytoplasmic envelopment of HCMV and showed a novel FIP4 function independent of Arf5 or Arf6 activity." @default.
• W2032067173 created "2016-06-24" @default.
• W2032067173 creator A5010294666 @default.
• W2032067173 creator A5070304125 @default.
• W2032067173 creator A5082458929 @default.
• W2032067173 date "2009-09-10" @default.
• W2032067173 modified "2023-10-14" @default.
• W2032067173 title "HCMV-Encoded Glycoprotein M (UL100) Interacts with Rab11 Effector Protein FIP4" @default.
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• W2032067173 doi "https://doi.org/10.1111/j.1600-0854.2009.00967.x" @default.
• W2032067173 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4118585" @default.
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