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Ini1/hSNF5 is dispensable for retrovirus-induced cytoplasmic accumulation of PML and does not interfere with integration

Retroviral infection triggers the cytoplasmic translocation of two Crm1-dependent shuttle factors, namely the Ini1 (integrase interactor 1, hSNF5) and the promyelocytic leukemia (PML) protein. Blocking nuclear export of shuttle factors by leptomycin B increases the efficiency of retroviral integrati...

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Published in:FEBS letters 2004-12, Vol.578 (3), p.291-296
Main Authors: Boese, Annette, Sommer, Peter, Gaussin, Armelle, Reimann, Andreas, Nehrbass, Ulf
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cited_by cdi_FETCH-LOGICAL-c4978-f2164d42269f91e1c30e7687b48341622fc78370420187e6f362c36be65f8c673
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creator Boese, Annette
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description Retroviral infection triggers the cytoplasmic translocation of two Crm1-dependent shuttle factors, namely the Ini1 (integrase interactor 1, hSNF5) and the promyelocytic leukemia (PML) protein. Blocking nuclear export of shuttle factors by leptomycin B increases the efficiency of retroviral integration, suggesting that some may mediate antiviral activity. While PML was shown to counteract proviral establishment, it remained unclear whether Ini1, a protein implicated in various processes during human immunodeficiency virus replication, has the same potential. Employing RNA interference-mediated knock-down of Ini1, we show here that the simultaneous accumulation of both proteins in the cytoplasm likely reflects two non-interdependent phenomena. Furthermore, Ini1 does not interfere with retroviral integration, as cells lacking Ini1 show no increased infection susceptibility.
doi_str_mv 10.1016/j.febslet.2004.11.016
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Blocking nuclear export of shuttle factors by leptomycin B increases the efficiency of retroviral integration, suggesting that some may mediate antiviral activity. While PML was shown to counteract proviral establishment, it remained unclear whether Ini1, a protein implicated in various processes during human immunodeficiency virus replication, has the same potential. Employing RNA interference-mediated knock-down of Ini1, we show here that the simultaneous accumulation of both proteins in the cytoplasm likely reflects two non-interdependent phenomena. 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ispartof FEBS letters, 2004-12, Vol.578 (3), p.291-296
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subjects Annexin A5
Annexin A5 - metabolism
Antibiotics, Antineoplastic
Antibiotics, Antineoplastic - pharmacology
Blotting, Western
Cell Fractionation
Chromosomal Proteins, Non-Histone
Cytoplasm
Cytoplasm - metabolism
DNA-Binding Proteins
DNA-Binding Proteins - drug effects
DNA-Binding Proteins - metabolism
double-stranded RNA
dsRNA
EGFP
enhanced green fluorescence protein
FACS
Fatty Acids, Unsaturated
Fatty Acids, Unsaturated - pharmacology
fluorescence activated cell sorting
Fluorescent Antibody Technique
HeLa Cells
HIV
Human immunodeficiency virus
Humans
Ini1
integrase interactor 1
Integrase interactor 1/hSNF5
leptomycin B
Life Sciences
LMB
Microbiology and Parasitology
Neoplasm Proteins
Neoplasm Proteins - biosynthesis
Neoplasm Proteins - drug effects
Nuclear Proteins
Nuclear Proteins - biosynthesis
Nuclear Proteins - drug effects
PBS
phosphate-buffered saline
PIC
PML
PML oncogenic domain
POD
Polymerase Chain Reaction
preintegration complex
Promyelocytic Leukemia Protein
propidium iodide
Retroviral integration
Retroviridae Infections
Retroviridae Infections - enzymology
Retroviridae Infections - metabolism
RNA Interference
RNAi
siRNA
small inhibitory RNA
SMARCB1 Protein
Transcription Factors
Transcription Factors - biosynthesis
Transcription Factors - drug effects
Tumor Suppressor Proteins
vesicular stomatitis virus glycoprotein
Virology
Virus Integration
Virus Integration - physiology
VSV-G
wild type
title Ini1/hSNF5 is dispensable for retrovirus-induced cytoplasmic accumulation of PML and does not interfere with integration
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