ArticleNucleic acids research2010
Transcription regulation of caspase-1 by R393 of HIPPI and its molecular partner HIP-1.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 14 citations in OpenAlex.
- The ubiquitin ligase FBXW7 regulates epithelial pyroptosis in severe asthma.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026Article
- Phosphorylation of Ku70 subunit by cell cycle kinases modulates the replication related function of Ku heterodimer.Nucleic acids research · 2016Article
- Article
- Epigonal conditioned media from bonnethead shark, Sphyrna tiburo, induces apoptosis in a T-cell leukemia cell line, Jurkat E6-1.Marine drugs · 2013Article
- Grb2 is regulated by foxd3 and has roles in preventing accumulation and aggregation of mutant huntingtin.PloS one · 2013Article
- The expression of caspases is enhanced in peripheral blood mononuclear cells of autism spectrum disorder patients.Journal of autism and developmental disorders · 2012Article
- Regulation of RE1 protein silencing transcription factor (REST) expression by HIP1 protein interactor (HIPPI).The Journal of biological chemistry · 2011Article
- Genome wide gene expression regulation by HIP1 Protein Interactor, HIPPI: prediction and validation.BMC genomics · 2011Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Earlier we have shown that exogenous expression of HIPPI, a molecular partner of Huntingtin interacting protein HIP-1, induces apoptosis and increases expression of caspases-1, -8 and -10 in HeLa and Neuro2A cells. The C-terminal pseudo death effector domain of HIPPI (pDED-HIPPI) specifically interacts with the putative promoter sequences of these genes. In the present manuscript, we predict from structural modeling of pDED-HIPPI that R393 of HIPPI is important for such interaction. R393E mutation in pDED-HIPPI decreases the interaction with the putative promoter of caspase-1 in cells. Expression of caspase-1 is decreased in cells expressing mutant pDED-HIPPI in comparison to that observed in cells expressing wild type pDED-HIPPI. Using HIP-1 knocked down cells as well as over expressing HIP-1 with mutation at its nuclear localization signal and other deletion mutations, we demonstrate that translocation of HIPPI to the nucleus is mediated by HIP-1 for the increased expression of caspase-1. HIPPI-HIP-1 heterodimer is detected in cytoplasm as well as in the nucleus and is associated with transcription complex in cells. Taking together, we are able to show the importance of R393 of HIPPI and the role of HIPPI-HIP-1 heterodimer in the transcription regulation of caspase-1.
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