Premium
HCMV‐Encoded Glycoprotein M (UL100) Interacts with Rab11 Effector Protein FIP4
Author(s) -
Krzyzaniak Magdalena A.,
Mach Michael,
Britt William J.
Publication year - 2009
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1111/j.1600-0854.2009.00967.x
Subject(s) - biology , glycoprotein , microbiology and biotechnology , effector , endosome , human cytomegalovirus , cytoplasm , virology , membrane glycoproteins , virus , intracellular
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.