Ask about this productRelated genes to: SIAH3 Blocking Peptide
- Gene:
- SIAH3 NIH gene
- Name:
- siah E3 ubiquitin protein ligase family member 3
- Previous symbol:
- -
- Synonyms:
- FLJ39203
- Chromosome:
- 13q14.13
- Locus Type:
- gene with protein product
- Date approved:
- 2008-12-05
- Date modifiied:
- 2019-03-19
Related products to: SIAH3 Blocking Peptide
Related articles to: SIAH3 Blocking Peptide
- Hypercapnia is a key feature of the respiratory microenvironment in many pathologic conditions. It occurs both as a regional and as a systemic process, and it is associated with multiple metabolic changes such as mitochondrial dysfunction, decreased ATP production, and metabolic shift from glycolytic energy production to fatty acid metabolism. In the cancer tumor microenvironment, hypercapnia has been linked at times to enhanced cell migration, invasion, and chemoresistance. Our previous work has shown that hypercapnia-associated gene signatures can be used as prognostic biomarkers. However, unlike the hypoxia-inducible factor pathway, there are no validated targets to quantify hypercapnia. In this study, we investigated the phenotypic and transcriptomic changes occurring in pancreatic ductal adenocarcinoma (PDAC) due to chronic exposure to hypercapnic atmospheres. We then identified and validated SIAH3 as a hypercapnia-affected target and explored its clinical relevance as a prognostic factor in PDAC. - Source: PubMed
Publication date: 2025/03/21
Zohar NitzanMaguire RyanKhalilieh SaedJain AditiBosykh DmitriyBowne Wilbur BLavu HarishYeo Charles JNevler Avinoam - Acute promyelocytic leukemia (APL) accounts for approximately 10-15% of newly diagnosed acute myeloid leukemia cases and presents with coagulopathy and bleeding. Prompt diagnosis and treatment are required to minimize early mortality in APL as initiation of all-trans retinoic acid therapy rapidly reverses coagulopathy. The fusion is a hallmark of APL and its rapid identification is essential for rapid initiation of specific treatment to prevent early deaths from coagulopathy and bleeding and optimize patient outcomes. Given limitations and long turnaround time of current gene fusion diagnostic strategies, we have developed a novel amplification-free nanopore sequencing-based approach with low cost, easy setup, and fast turnaround time. We termed the approach CRISPR/Cas9-enriched nanopore sequencing with adaptive sampling (CENAS). Using CENAS, we successfully sequenced breakpoints of typical and atypical fusions in APL patients. Compared with the standard-of-care genetic diagnostic tests, CENAS achieved good concordance in detecting fusions in this study. CENAS allowed for the identification of sequence information of fusion breakpoints involved in typical and atypical fusions and identified additional genes ( and ) and genomic regions (13q14.13) involving the atypical fusions. To the best of our knowledge, involvements of the gene, the gene, and the 13q14.13 genomic region flanking with the and genes have not been reported in the atypical fusions. CENAS has great potential to develop as a point-of-care test enabling immediate, low-cost bedside diagnosis of APL patients with a fusion. Given the early death rate in APL patients still reaches 15%, and ~10% of APL patients are resistant to initial therapy or prone to relapse, further sequencing studies of typical and atypical fusion might shed light on the pathophysiology of the disease and its responsiveness to treatment. Understanding the involvement of additional genes and positional effects related to the and genes could shed light on their role in APL and may aid in the development of novel targeted therapies. - Source: PubMed
Publication date: 2024/12/13
Middlezong WilliamStinnett VictoriaPhan MichaelPhan BrianMorsberger LauraKlausner MelanieGhabrial JenDeMetrick NatalieZhu JingJames TrishaPallavajjala AparnaGocke Christopher DBaer Maria RZou Ying S - Developmental axon pruning is controlled by a careful balance of pro- and anti-apoptotic signals, which are activated in response to external cues to sculpt mature neuronal circuitry. In this issue of , Abraham define a safeguard against apoptotic axon pruning and illustrate that Siah3 represses Parkin-mediated mitophagy to control the availability of axonal mitochondria that activate the pruning process. - Source: PubMed
Publication date: 2024/10/08
Davidson Rina LSimon David J - Mitophagy eliminates dysfunctional mitochondria, and defects in this cellular housekeeping mechanism are implicated in various age-related diseases. Here, we found that mitophagy suppression by the protein Siah3 promoted developmental axonal remodeling in mice. Siah3-deficient mice displayed increased peripheral sensory innervation. Cultured Siah3-deficient sensory neurons exhibited delays in both axonal degeneration and caspase-3 activation in response to withdrawal of nerve growth factor. Mechanistically, Siah3 was transcriptionally induced by the loss of trophic support and formed a complex with the cytosolic E3 ubiquitin ligase parkin, a core component of mitophagy, in transfected cells. Axons of Siah3-deficient neurons mounted profound mitophagy upon initiation of degeneration but not under basal conditions. Neurons lacking both Siah3 and parkin did not exhibit the delay in trophic deprivation-induced axonal degeneration or the induction of axonal mitophagy that was seen in Siah3-deficient neurons. Our findings reveal that mitophagy regulation acts as a gatekeeper of a physiological axon elimination program. - Source: PubMed
Publication date: 2024/10/08
Abraham OmerBen-Dor ShifraGoliand InnaHaffner-Krausz RebeccaColaiuta Sarah PhoebelucKovalenko AndrewYaron Avraham - Of the seven in absentia homologue (SIAH) family, three members have been identified in the human genome. In contrast to the E3 ubiquitin ligase encoding SIAH1 and SIAH2, little is known on the regulation and function of SIAH3 in tumorigenesis. In this study, we reveal that SIAH3 is frequently epigenetically silenced in different cancer entities, including cutaneous melanoma, lung adenocarcinoma and head and neck cancer. Low SIAH3 levels correlate with an impaired survival of cancer patients. Additionally, induced expression of SIAH3 reduces cell proliferation and induces cell death. Functionally, SIAH3 negatively affects cellular metabolism by shifting cells form aerobic oxidative phosphorylation to glycolysis. SIAH3 is localized in the mitochondrion and interacts with proteins involved in mitochondrial ribosome biogenesis and translation. We also report that SIAH3 interacts with ubiquitin ligases, including SIAH1 or SIAH2, and is degraded by them. These results suggest that SIAH3 acts as an epigenetically controlled tumor suppressor by regulating cellular metabolism through the inhibition of oxidative phosphorylation. - Source: PubMed
Publication date: 2024/09/30
Deutschmeyer Verena ESchlaudraff Nico AWalesch Sara KMoyer JanineSokol Anna MGraumann JohannesMeissner WolfgangSchneider MarcMuley ThomasHelmbold PeterSchwinn MarkusRichter Antje MSchmitz M LienhardDammann Reinhard H