Replication interactions
Interaction |
Pubs |
HIV-1 replication requires amino acids 896-1475 in NUP153; deletion of the c-terminal domain of NUP153 amino acid stretch disrupts viral infectivity |
PubMed
|
HIV-1 replication requires NUP153 for import into the nucleus as shown through shRNA treatment |
PubMed
|
Knockdown of CPSF6, TNPO3, or NUP153 through siRNA leads to decreased CA and proviral DNA nuclear entry |
PubMed
|
Depletion of nucleoporin 153kDa (NUP153) by shRNA inhibits HIV-1 infection in human Jurkat lymphocytes |
PubMed
|
HIV-1 requires NUP153 and TPR for infectivity as shown by shRNA knockdown experiments utilizing HeLa-derived P4-CCR5 cells and jurkat T cells |
PubMed
|
shRNA knockdown of NUP153 renders cells less permissive to HIV-1 WT; HIV-1 is enhanced by NUP153 |
PubMed
|
Knockdown of nucleoporin 153kDa (NUP153) by siRNA inhibits HIV-1 replication in HeLa-derived TZM-bl cells |
PubMed
|
Knockdown of nucleoporin 153kDa (NUP153) by siRNA inhibits the early stages of HIV-1 replication in 293T cells infected with VSV-G pseudotyped HIV-1 |
PubMed
|
Protein interactions
Protein |
Gene |
Interaction |
Pubs |
Rev
|
rev
|
antibodies to nup153 can block the nuclear export of Rev as well as Rev-dependent RNA export |
PubMed
|
|
rev
|
nup153 is involved in Rev-mediated nuclear export of HIV-1 mRNA through an interaction with eukaryotic initiation factor 5A (eIF-5A) which binds to Rev |
PubMed
|
Tat
|
tat
|
Interaction of HIV-1 Tat with Nup153 in T-cells is identified by a proteomic strategy based on affinity chromatography |
PubMed
|
Vpr
|
vpr
|
HIV-1 Vpr co-immunoprecipitates in vitro-translated human Nup153 |
PubMed
|
capsid
|
gag
|
HIV-1 CA binds NUP153; HIV-1 CA mutations S41A, Q67H, V165I and V172I in combination abrogate this interaction |
PubMed
|
|
gag
|
HIV-1 CA interacts with NUP153, which is required for replication |
PubMed
|
|
gag
|
Full-length NUP153 binids to the CA hexamer with lower affinity compared with the CPSF6 peptide |
PubMed
|
|
gag
|
Amino-acid residues 1199-1475 in the C-terminal phenylalanine-glycine motifs of NUP153 are involved in the binding to HIV-1 CA. Mutation of CA Asn74 to Ala diminishes the binding, while mutation to Asp enhances the binding |
PubMed
|
|
gag
|
Nucleoporins NUP153 and NUP98 bind in vitro assembled HIV-1 CA-NC complexes, suggesting that both nucleoporins bind the HIV-1 core during the early stages of infection |
PubMed
|
|
gag
|
HIV-1 CA mutant N74D and depletion of NUP153 and LEDGF/p75 significantly reduce HIV-1 DNA integration into gene-rich regions of chromosomes and gene bodies |
PubMed
|
integrase
|
gag-pol
|
Depletion of the nuclear pore complex component NUP153 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 NUP153 in cells |
PubMed
|
|
gag-pol
|
NUP153 dependency during HIV-1 infection is dependent on HIV-1 integrase (IN) |
PubMed
|
|
gag-pol
|
NTF2 is enriched at the nuclear envelope and interacts with NUP153, When added in excess to the import assay, NUP153C inhibited the nuclear import of IN. |
PubMed
|
|
gag-pol
|
HIV-1 IN binds directly to nucleoporin NUP153 in cells. The binding involves the C-terminal FxFG-rich region of NUP153 |
PubMed
|
nucleocapsid
|
gag
|
Nucleoporins NUP153 and NUP98 bind in vitro assembled HIV-1 CA-NC complexes, suggesting that both nucleoporins bind the HIV-1 core during the early stages of infection |
PubMed
|
Go to the HIV-1, Human Interaction Database