SLC25A3 Antibody (Center) Blocking Peptide
- Known as:
- SLC25A3 Antibody (Center) Blocking Peptide
- Catalog number:
- BP17106c
- Product Quantity:
- 2
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- SLC25A3 Antibody (Center) Blocking Peptide
Related genes to: SLC25A3 Antibody (Center) Blocking Peptide
- Gene:
- SLC25A3 NIH gene
- Name:
- solute carrier family 25 member 3
- Previous symbol:
- PHC
- Synonyms:
- -
- Chromosome:
- 12q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 1993-05-14
- Date modifiied:
- 2016-02-18
Related products to: SLC25A3 Antibody (Center) Blocking Peptide
Related articles to: SLC25A3 Antibody (Center) Blocking Peptide
- Copper (Cu) is an essential cofactor for cytochrome oxidase (CcO), a mitochondrial respiratory chain enzyme that is metalated in the intermembrane space (IMS) primarily using Cu derived from the mitochondrial matrix pool. While Cu import into the matrix depends on the inner membrane carrier SLC25A3, the route by which matrix Cu is exported to the IMS for insertion into CcO has remained a major, unresolved step in intramitochondrial Cu trafficking. Here, we leveraged our recent discovery that the Cu ionophore elesclomol (ES) releases Cu directly into the mitochondrial matrix to show that SLC25A3 is required for exporting Cu to the IMS for CcO metalation. Loss of SLC25A3 decreases mitochondrial Cu content and CcO activity as expected. Strikingly, bypassing the loss of SLC25A3 with ES-mediated Cu delivery to the matrix fails to restore CcO function; rather, it drives toxic Cu retention and triggers cuproptosis, revealing that SLC25A3-facilitated Cu export is the limiting determinant of CcO metalation. Heterologous expression in confirms that SLC25A3 can mediate Cu export. These results suggest that SLC25A3 is the long-sought mitochondrial Cu exporter with a dual role in enabling CcO metalation and gating susceptibility to cuproptosis. - Source: PubMed
Publication date: 2026/06/17
Zulkifli MohammadFarid IfrahOldfather Laura EShanbhag Vinit CLeary Scot CPetris Michael JCobine Paul AGohil Vishal M - Differentiation of skeletal muscle is associated with increased mitochondrial biogenesis and reliance of oxidative phosphorylation (OXPHOS). The terminal enzyme complex in the electron transport chain, cytochrome c oxidase (COX), requires copper for its assembly and activity, and copper delivery to mitochondria is essential for OXPHOS. However, when mitochondrial copper becomes essential during skeletal myoblast differentiation is not known. Here, we show that genetic deficiency of the mitochondrial copper and phosphate carrier SLC25A3 induced prior to myoblast differentiation leads to the formation of smaller myotubes, but SLC25A3 deficiency induced in mature myotubes leads to cell death and detachment. Both phenotypes are recapitulated upon genetic knockdown of COX17, a critical assembly protein for both COX copper cofactors, or by chemical inhibition of COX. Importantly, myotube death caused by SLC25A3 deficiency is rescued by copper supplementation or expression of an SLC25A3 variant that transports copper but not phosphate. Taken together these data support a model wherein copper transport by SLC25A3 and copper delivery to COX is critical for survival in mature myotubes. - Source: PubMed
Publication date: 2026/06/07
Perez Alexandra MFivush Jason DCordill Bailey MFerguson NathanZhang YuMezzell Allison TMattam UshodayaChaudhry OmarPorter Karleigh GMaadaadi SaanviSecic DinaBischoff MeganChella Krishnan KarthickeyanKovall RhettCunningham TomCzyzyk-Krzeska MariaVest Katherine E - Copper (Cu) is an essential cofactor for mitochondrial cytochrome oxidase, yet whether it directly regulates mitochondrial metabolism beyond respiration remains unclear. Here we show that mitochondrial Cu, delivered by SLC25A3, is required to maintain the stability of lipoylated TCA cycle proteins. Loss of or pharmacological Cu depletion selectively destabilized the lipoylated E2 subunits of mitochondrial dehydrogenases and the lipoylation enzymes LIPT1 and LIPT2, an effect not reproduced by acute electron transport chain inhibition. Mechanistically, we find that Cu directly engages the reduced lipoyl moiety using chemical probes and synthetic peptide approaches. Cu depletion impaired PDH and OGDH activity, rewired TCA cycle metabolism, and imposed a dependence on pyruvate carboxylase for anaplerosis. This metabolic defect depleted aspartate, suppressed mTORC1 signaling, and limited proliferation. Conversely, selective delivery of Cu to the mitochondria restored lipoylation, TCA cycle function, and cell growth. Together, these findings identify mitochondrial Cu as a structural regulator of the lipoylation machinery and reveal a direct link between Cu homeostasis and central carbon metabolism. - Source: PubMed
Publication date: 2026/05/22
Ghosh SantanuJarvis Andrew FHintzen Jordi C JMcKnight Nate RCosta-Pinheiro PedroNoughton Noelle HKim YumiJaccard AlisonLeary Scot CCobine Paul ABartman Caroline RDeNicola Gina MSnyder Nathaniel WWellen Kathryn EBurslem George MBrady Donita C - Cuproptosis is defined as a novel form of regulated cell death triggered by copper accumulation, with emerging evidence linking cuproptosis-related genes (CRGs) to tumor progression. However, the prognostic relevance of CRGs in papillary renal cell carcinoma (PRCC) remains elusive. This study aimed to construct and validate a cuproptosis-related gene prognostic signature for PRCC, and to explore its potential value in risk stratification, immune infiltration, and pathogenesis. - Source: PubMed
Li HaixiaCao LiLi RuiminXu LingZhang ShuxiaGao JianjunChen YongxueLian Xiaoqiang - Mitochondria divide and fuse, and the balance between these processes maintains mitochondrial morphology and function. Although the core fusion and division machinery is well established, how cells sense mitochondrial morphology and actively adjust it remains unclear. In this Opinion article, we propose a new conceptual framework, termed 'Mitochondrial Safeguard (MitoSafe)', in which cells monitor mitochondrial size and rebalance division and fusion through four branches: activation of fusion or inhibition of division in small mitochondria and activation of division or inhibition of fusion in enlarged mitochondria. Recent findings show that fusion is suppressed once mitochondria exceed a healthy size threshold. Dysregulation of this branch of MitoSafe, involving Parkin, PINK1, SLC25A3, SOD1, and cytochrome-c oxidase, causes mitochondrial enlargement, mitochondrial DNA release, and stimulator of interferon genes (STING)-mediated inflammation. - Source: PubMed
Publication date: 2026/05/13
Haggerty NoraNakamura KentaroSesaki HiromiIijima Miho