Regulated nuclear import of the STAT1 transcription factor by direct binding of importin‐α
By Kevin M. McBride, Gregg Banninger, C. McDonald, N. Reich. 2002
302 citations recorded by the source corpus.
Subfields: Molecular Biology, Oncology
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Citations in the corpus
- Regulation of JAK–STAT signalling in the immune system (2003, background): “Recently, it has been shown that tyrosine phosphorylated STAT1 needs to be dephosphorylated to leave the nucleus, indicating a role for tyrosine phosphorylation in the nuclear retention of STAT1 (Ref”
- STAT proteins: From normal control of cellular events to tumorigenesis (2003, background): “Binding of STAT1 to importin-a5, one of the subunits of the nucleocytoplasmic transport machinery, has been described, and recent studies indicated that L407, K410, and K413 in STAT1 are critical residues in the nuclear import of tyrosine-phosphorylated STAT1 (McBride et al., 2002).”
- SARS-CoV-2 Orf6 hijacks Nup98 to block STAT nuclear import and antagonize interferon signaling (2020, background): “S7, both KPNA1 and KPNA2 localized to the nucleus in Orf6M58R-expressing cells, indicating that the SARS-CoV-2dependent cytoplasmic accumulation of the KPNAs is likely a result of the impaired nucleocytoplasmic trafficking due to the Orf6-Nup98 interaction.”
- Signalling: STATs: transcriptional control and biological impact (2002, unknown): “cgi?l=3836">importin-α5 , one of the subunits of the nucleocytoplasmic transport machinery, has been describe”
- Severe Acute Respiratory Syndrome Coronavirus ORF6 Antagonizes STAT1 Function by Sequestering Nuclear Import Factors on the Rough Endoplasmic Reticulum/Golgi Membrane (2007, background): “ISGF3 binds import factor karyopherin alpha 1 (KPNA1) and recruits karyopherin beta 1 (KPNB1) for transport into the nucleus (35), where STAT1 acts as a transcription factor for many IFN-induced genes that establish the antiviral state (34, 36).”