ArticleProceedings of the National Academy of Sciences of the United States of America2006
Site-specific proteolysis of the transcriptional coactivator HCF-1 can regulate its interaction with protein cofactors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 24 citations in OpenAlex.
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- Mammalian cell proliferation requires noncatalytic functions of O-GlcNAc transferase.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- JMJD5 cleaves monomethylated histone H3 N-tail under DNA damaging stress.EMBO reports · 2017Article
- Inhibition of O-Linked N-Acetylglucosamine Transferase Reduces Replication of Herpes Simplex Virus and Human Cytomegalovirus.Journal of virology · 2015Article
- Article
- Host cell factor-1 recruitment to E2F-bound and cell-cycle-control genes is mediated by THAP11 and ZNF143.Cell reports · 2014Article
- The dynamics of HCF-1 modulation of herpes simplex virus chromatin during initiation of infection.Viruses · 2013Review
- Targeting the JMJD2 histone demethylases to epigenetically control herpesvirus infection and reactivation from latency.Science translational medicine · 2013Article
- Crosstalk between O-GlcNAcylation and proteolytic cleavage regulates the host cell factor-1 maturation pathway.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Transcriptional coactivator HCF-1 couples the histone chaperone Asf1b to HSV-1 DNA replication components.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Cathepsin L proteolytically processes histone H3 during mouse embryonic stem cell differentiation.Cell · 2008Article
- Association of the cellular coactivator HCF-1 with the Golgi apparatus in sensory neurons.Journal of virology · 2008Article
- Species selectivity of mixed-lineage leukemia/trithorax and HCF proteolytic maturation pathways.Molecular and cellular biology · 2007Article
- The coactivator host cell factor-1 mediates Set1 and MLL1 H3K4 trimethylation at herpesvirus immediate early promoters for initiation of infection.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Further characterization of the signaling proteolysis step in the Aspergillus nidulans pH signal transduction pathway.Eukaryotic cell · 2007Article
- Control of alpha-herpesvirus IE gene expression by HCF-1 coupled chromatin modification activities.Biochimica et biophysica actaReview
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Limited proteolytic processing is an important transcriptional regulatory mechanism. In various contexts, proteolysis controls the cytoplasmic-to-nuclear transport of important transcription factors or removes domains to produce factors with altered activities. The transcriptional coactivator host cell factor-1 (HCF-1) is proteolytically processed within a unique domain consisting of 20-aa reiterations. Site-specific cleavage within one or more repeats generates a family of amino- and carboxyl-terminal subunits that remain tightly associated. However, the consequences of HCF-1 processing have been undefined. In this study, it was determined that the HCF-1-processing domain interacts with several proteins including the transcriptional coactivator/corepressor four-and-a-half LIM domain-2 (FHL2). Analysis of this interaction has uncovered specificity with both sequence and context determinants within the reiterations of this processing domain. In cells, FHL2 interacts exclusively with the nonprocessed coactivator and costimulates transcription of an HCF-1-dependent target gene. The functional interaction of HCF-1 with FHL2 supports a model in which site-specific proteolysis regulates the interaction of HCF-1 with protein partners and thus can modulate the activity of this coactivator. This paradigm expands the biological significance of limited proteolytic processing as a regulatory mechanism in gene transcription.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.