Replication interactions
Interaction |
Pubs |
HIV-1 replication, specifically uncoating and nuclear import, requires RANBP2 (NUP358) and KIF5B as shown through siRNA knockdown of each protein |
PubMed
|
shRNA knockdown of RANBP2 renders cells less permissive to HIV-1 WT; HIV-1 is enhanced by RANBP2 [HOWEVER HIV-1 with CA mutations S41A, Q67H, V165I and V172I in combination and/or CA mutation N74D exhibit reduced dependence on RANBP2 for infectivity] |
PubMed
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Knockdown of RAN binding protein 2 (RANBP2) by siRNA inhibits HIV-1 replication in HeLa-derived TZM-bl cells |
PubMed
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Knockdown of RAN binding protein 2 (RANBP2) by siRNA inhibits the early stages of HIV-1 replication in 293T cells infected with VSV-G pseudotyped HIV-1 |
PubMed
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Protein interactions
Protein |
Gene |
Interaction |
Pubs |
Rev
|
rev
|
SiRNA-mediated depletion of RanBP2 impairs biological activities of ectopically expressed HIV-1 Tat and Rev proteins. RanBP2 depletion also inhibits HIV-1 replication by blocking nuclear import of HIV-1 DNA PIC |
PubMed
|
Tat
|
tat
|
Interaction of HIV-1 Tat with Nup358 in T-cells is identified by a proteomic strategy based on affinity chromatography |
PubMed
|
|
tat
|
SiRNA-mediated depletion of RanBP2 impairs biological activities of ectopically expressed HIV-1 Tat and Rev proteins. RanBP2 depletion also inhibits HIV-1 replication by blocking nuclear import of HIV-1 DNA PIC |
PubMed
|
capsid
|
gag
|
HIV-1 CA relocalizes RANBP2 (NUP358) into the cytoplasm of infected cells |
PubMed
|
|
gag
|
NUP358 is involved in HIV-1 nuclear entry and HIV-1 CA protein is the determinant for NUP358-dependent nuclear import |
PubMed
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|
gag
|
HIV-1 CA mutants N74D and P90A fail to bind to CPSF6 and cyclophilins (Nup358 and CypA), respectively, and trigger innate sensors, leading to nuclear translocation of NFkappaB and IRF3, production of type 1 IFN and induction of an antiviral state |
PubMed
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|
gag
|
HIV-1 CA mutant virus N74D infection is inhibited in the Nup358 null cells, but rescued by Nup358 (1-1340) expression |
PubMed
|
|
gag
|
Residues N57, M66, Q67, K70, N74, and T107 in the N-terminal domain of HIV-1 CA are important for the binding to CPSF6. Mutations on these residues lead to the loss or reduction of dependency on TNPO3 and RanBP2 |
PubMed
|
|
gag
|
CypA-CA interactions dictate the use of a NUP358/NUP153 dependent nuclear entry pathway |
PubMed
|
|
gag
|
The crystal structure of the C-terminal domain (CTD; residues 3062-3224) of NUP358 reveals that the CTD possesses weak peptidyl-prolyl isomerase activity and mediates a weak association with CA. The V3173W mutant abolishes its association with CA |
PubMed
|
|
gag
|
NUP358 V61M mutation abolishes its interaction with the HIV-1 CA N-terminal domain, while V113F preserves its binding to CA |
PubMed
|
|
gag
|
NUP358 interacts with HIV-1 CA via its cyclophilin domain (residues 3064-3222). Replacement of HIV-1 CA with SIVmac CA renders HIV-1 largely insensitive to NUP358 depletion |
PubMed
|
integrase
|
gag-pol
|
Depletion of the nuclear transport factor RANBP2 by RNAi blocks HIV-1 nuclear import and integration efficiency as assayed by the appearance of circular viral DNAs, suggesting HIV-1 IN interacts with RANBP2 in cells |
PubMed
|
Go to the HIV-1, Human Interaction Database