Abstract:
:The HIV-1 protein Vpr enhances macrophage infection, triggers G2 cell cycle arrest, and targets cells for NK-cell killing. Vpr acts through the CRL4(DCAF1) ubiquitin ligase complex to cause G2 arrest and trigger expression of NK ligands. Corresponding ubiquitination targets have not been identified. UNG2 and SMUG1 are the only known substrates for Vpr-directed depletion through CRL4(DCAF1). Here we identify the endoribonuclease Dicer as a target of HIV-1 Vpr-directed proteasomal degradation through CRL4(DCAF1). We show that HIV-1 Vpr inhibits short hairpin RNA function as expected upon reduction of Dicer levels. Dicer inhibits HIV-1 replication in T cells. We demonstrate that Dicer also restricts HIV-1 replication in human monocyte-derived macrophages (MDM) and that reducing Dicer expression in MDMs enhances HIV-1 infection in a Vpr-dependent manner. Our results support a model in which Vpr complexes with human Dicer to boost its interaction with the CRL4(DCAF1) ubiquitin ligase complex and its subsequent degradation.
journal_name
Virologyjournal_title
Virologyauthors
Casey Klockow L,Sharifi HJ,Wen X,Flagg M,Furuya AK,Nekorchuk M,de Noronha CMdoi
10.1016/j.virol.2013.06.010subject
Has Abstractpub_date
2013-09-01 00:00:00pages
191-202issue
1-2eissn
0042-6822issn
1096-0341pii
S0042-6822(13)00359-0journal_volume
444pub_type
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