ArticleMolecular and cellular biology2003
The human I-mfa domain-containing protein, HIC, interacts with cyclin T1 and modulates P-TEFb-dependent transcription.
Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 46 citations in OpenAlex.
- Transcriptional pause release at enhancers mediates cell identity.NAR cancer · 2025Review
- I-mfa, Mesangial Cell TRPC1 Channel, and Regulation of GFR.Journal of the American Society of Nephrology : JASN · 2025Article
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- Multiple information carried by RNAs: total eclipse or a light at the end of the tunnel?RNA biology · 2020Review
- Non coding RNAs as the critical factors in chemo resistance of bladder tumor cells.Diagnostic pathology · 2020Review
- Positive Regulation of Transcription by Human ZMYND8 through Its Association with P-TEFb Complex.Cell reports · 2018Article
- Cross-talk between the glucocorticoid receptor and MyoD family inhibitor domain-containing protein provides a new mechanism for generating tissue-specific responses to glucocorticoids.The Journal of biological chemistry · 2017Article
- Mechanisms and Developmental Roles of Promoter-proximal Pausing of RNA Polymerase II.Journal of stem cell research & therapy · 2016Article
- The DNA methylation-regulated miR-193a-3p dictates the multi-chemoresistance of bladder cancer via repression of SRSF2/PLAU/HIC2 expression.Cell death & disease · 2014Article
- Differential host cell gene expression and regulation of cell cycle progression by nonstructural protein 11 of porcine reproductive and respiratory syndrome virus.BioMed research international · 2014Article
- The role of Rhox homeobox factors in tumorigenesis.Frontiers in bioscience (Landmark edition) · 2013Review
- Article
- HIV-1 replication and latency are regulated by translational control of cyclin T1.Journal of molecular biology · 2011Article
- Intermolecular masking of the HIV-1 Rev NLS by the cellular protein HIC: novel insights into the regulation of Rev nuclear import.Retrovirology · 2011Article
- Progranulin (granulin/epithelin precursor) and its constituent granulin repeats repress transcription from cellular promoters.Journal of cellular physiology · 2010Article
- Inhibition of HIV-1 gene expression by Ciclopirox and Deferiprone, drugs that prevent hypusination of eukaryotic initiation factor 5A.Retrovirology · 2009Article
- Article
- Involvement of the nucleolus in replication of human viruses.Reviews in medical virology · 2009Review
- The positive transcription elongation factor b is an essential cofactor for the activation of transcription by myocyte enhancer factor 2.Journal of molecular biology · 2008Article
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4 authors at 1 institution.
Funding
Abstract
Positive transcription elongation factor b (P-TEFb) hyperphosphorylates the carboxy-terminal domain of RNA polymerase II, permitting productive transcriptional elongation. The cyclin T1 subunit of P-TEFb engages cellular transcription factors as well as the human immunodeficiency virus type 1 (HIV-1) transactivator Tat. To identify potential P-TEFb regulators, we conducted a yeast two-hybrid screen with cyclin T1 as bait. Among the proteins isolated was the human I-mfa domain-containing protein (HIC). HIC has been reported to modulate expression from both cellular and viral promoters via its C-terminal cysteine-rich domain, which is similar to the inhibitor of MyoD family a (I-mfa) protein. We show that HIC binds cyclin T1 in yeast and mammalian cells and that it interacts with intact P-TEFb in mammalian cell extracts. The interaction involves the I-mfa domain of HIC and the regulatory histidine-rich region of cyclin T1. HIC also binds Tat via its I-mfa domain, although the sequence requirements are different. HIC colocalizes with cyclin T1 in nuclear speckle regions and with Tat in the nucleolus. Expression of the HIC cDNA modulates Tat transactivation of the HIV-1 long terminal repeat (LTR) in a cell type-specific fashion. It is mildly inhibitory in CEM cells but stimulates gene expression in HeLa, COS, and NIH 3T3 cells. The isolated I-mfa domain acts as a dominant negative inhibitor. Activation of the HIV-1 LTR by HIC in NIH 3T3 cells occurs at the RNA level and is mediated by direct interactions with P-TEFb.
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