Human immunodeficiency virus type 1 Vif induces cell cycle delay via recruitment of the same E3 ubiquitin ligase complex that targets APOBEC3 proteins for degradation.
Human immunodeficiency virus type 1 (HIV-1) Vif recruits a Cullin 5 ubiquitin ligase that targets APOBEC3 proteins for degradation. Recently, Vif has also been shown to induce cell cycle disturbance in G(2). We show that in contrast to the expression of Vpr, the expression of Vif does not preclude cell division, and therefore, Vif causes delay and not arrest in G(2). We also demonstrate that the interaction of Vif with the ubiquitin ligase is required for cell cycle disruption, as was previously shown for HIV-1 Vpr. The presence of APOBEC3 D/E, F, and G had no influence on Vif-induced alteration of the cell cycle. We conclude that cell cycle delay by Vif is a result of ubiquitination and degradation of a cellular protein that is different from the known APOBEC3 family members.
DeHart
Jason L
JL
Department of Pathology, University of Utah School of Medicine, 15 North Medical Drive East no. 2100, Room 2520, Salt Lake City, Utah 84112, USA.
Bosque
Alberto
A
Harris
Reuben S
RS
Planelles
Vicente
V
D000071478:APOBEC Deaminases; D002453:Cell Cycle / Q000187:drug effects; D002460:Cell Line; D003564:Cytidine Deaminase; D043525:Cytosine Deaminase / Q000378:metabolism*; D016195:G2 Phase / Q000187:drug effects*; D016346:Gene Products, vif / Q000378:metabolism / Q000494:pharmacology*; D015497:HIV-1 / Q000235:genetics / Q000378:metabolism / Q000472:pathogenicity*; D006801:Humans; D009154:Mutation; D014162:Transfection; D044767:Ubiquitin-Protein Ligases / Q000378:metabolism*
D016346:Gene Products, vif; D044767:Ubiquitin-Protein Ligases; D043525:Cytosine Deaminase; D000071478:APOBEC Deaminases; C502889:APOBEC3 proteins, human; D003564:Cytidine Deaminase