Protein interactions
Protein |
Gene |
Interaction |
Pubs |
integrase
|
gag-pol
|
Karyopherin alpha and beta are reported to interact with HIV-1 integrase (IN) to facilitate nuclear import of IN, however a conflicting report indicates nuclear accumulation of IN does not involve karyopherin alpha, beta 1, or beta 2 mediated pathways |
PubMed
|
|
gag-pol
|
HIV-1 IN interacts with importin alpha by the BiFC assay and amino acids 161-173 in IN are required for the interaction with importin alpha |
PubMed
|
|
gag-pol
|
HIV-1 Rev disrupts both IN-TNPO3 and IN-importin alpha complexes |
PubMed
|
|
gag-pol
|
Some reports indicate a possible role for the interactions between karyopherin alpha and beta with HIV-1 integrase in the nuclear import of HIV-1 preintegration complexes (PIC), while other reports indicate integrase is not involved in PIC nuclear import |
PubMed
|
|
gag-pol
|
Karyopherin alpha binds to a bipartite nuclear localization signal in HIV-1 integrase (amino acids 186-189 and 211-219) |
PubMed
|
matrix
|
gag
|
Nuclear import of HIV-1 preintegration complexes by karyopherin alpha is governed by phosphorylation of HIV-1 Matrix on tyrosine and serine, however the exact role of phosphorylation of the C-terminal tyrosine of Matrix has been debated |
PubMed
|
|
gag
|
HIV-1 Matrix increases intracellular ATP content, an effect hypothesized to support the ATP-dependent nuclear import of HIV-1 preintegration complexes by karyopherin alpha |
PubMed
|
|
gag
|
HIV-1 Vpr increases the affinity of karyopherin alpha to the HIV-1 Matrix nuclear localization signal, thereby mediating the nuclear import of HIV-1 preintegration complexes |
PubMed
|
|
gag
|
Hsp70 stimulates the binding of HIV-1 matrix to karyopherin alpha |
PubMed
|
|
gag
|
The role of HIV-1 Matrix during nuclear import of the HIV-1 preintegration complex has been controversial, however recent understanding indicates HIV-1 Matrix and Vpr proteins act in concert to facilitate nuclear import by binding to karyopherin alpha |
PubMed
|
|
gag
|
HIV-1 Matrix contains two nuclear localization signals (NLS) spanning amino acids 24-33 and 110-114 that are recognized by karyopherin alpha and mediate the nuclear import of HIV-1 preintegration complexes |
PubMed
|
Go to the HIV-1, Human Interaction Database