ArticleOncogene2007
A crosstalk between hSiah2 and Pias E3-ligases modulates Pias-dependent activation.
Article in Oncogene, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 22 citations in OpenAlex.
- B Cell Receptor Activation and Chemical Induction Trigger Caspase-Mediated Cleavage of PIAS1 to Facilitate Epstein-Barr Virus Reactivation.Cell reports · 2017Article
- The E3 ubiquitin ligase Siah1 regulates adrenal gland organization and aldosterone secretion.JCI insight · 2017Article
- Article
- Starting and stopping SUMOylation. What regulates the regulator?Chromosoma · 2013Review
- SUMO rules: regulatory concepts and their implication in neurologic functions.Neuromolecular medicine · 2013Review
- PIAS4 is an activator of hypoxia signalling via VHL suppression during growth of pancreatic cancer cells.British journal of cancer · 2013Article
- The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition.Nature reviews. Molecular cell biology · 2010Review
- PIAS proteins: pleiotropic interactors associated with SUMO.Cellular and molecular life sciences : CMLS · 2009Review
- Regulation of the sumoylation system in gene expression.Current opinion in cell biology · 2008Review
- SIAH-1 interacts with the Kaposi's sarcoma-associated herpesvirus-encoded ORF45 protein and promotes its ubiquitylation and proteasomal degradation.Journal of virology · 2008Article
- Nitric oxide destabilizes Pias3 and regulates sumoylation.PloS one · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Protein inhibitor of activated STAT (Pias) and human homologues of seven in absentia (hSiah) proteins both exhibit properties of ubiquitin-family peptides conjugating enzymes. Pias present E3-ligase activity for small ubiquitin-related modifiers (Sumo) covalent attachment to their targets. This post-translational modification is responsible for the activation of different transcription factors such as AP1. HSiah proteins possess ubiquitin-E3-ligase activity that triggers their partners to proteasomal-dependent degradation. The present study identifies Pias as a new hSiah2-interacting protein. We demonstrate that hSiah2 regulates specifically the proteasome-dependent degradation of Pias proteins. On reverse, Pias does not prevent hSiah2 degradation. We provide evidences for hSiah2-dependent degradation of Pias as being a mechanism in the regulation of c-jun N-terminal kinase-activating pathways. This report describes a new interconnection between sumoylation and ubiquitination pathways by regulating the levels of the E3-ligases available for these processes.
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Registered trials
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.