ATPAF2
- Known as:
- ATPAF2
- Catalog number:
- 002278A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ATPAF2
Related genes to: ATPAF2
- Gene:
- ATPAF2 NIH gene
- Name:
- ATP synthase mitochondrial F1 complex assembly factor 2
- Previous symbol:
- -
- Synonyms:
- Atp12p, ATP12, LP3663, MGC29736
- Chromosome:
- 17p11.2
- Locus Type:
- gene with protein product
- Date approved:
- 2002-07-01
- Date modifiied:
- 2014-11-18
Related products to: ATPAF2
Related articles to: ATPAF2
- Our current understanding of mitochondrial organelle physiology has benefited from two broad approaches: classically, cuvette-based measurements with suspensions of isolated mitochondria, in which bioenergetic parameters are monitored acutely in response to respiratory chain substrates and inhibitors, and more recently, highly scalable genetic screens for fitness phenotypes associated with coarse-grained properties of the mitochondrial state. Here we introduce permeabilized-cell mitochondrial function sequencing (PMF-seq) to combine strengths of these two approaches to connect genes to detailed bioenergetic phenotypes. In PMF-seq, the plasma membranes within a pool of CRISPR mutagenized cells are gently permeabilized under conditions that preserve mitochondrial physiology, where detailed bioenergetics can be probed in the same way as with isolated organelles. Cells with desired bioenergetic parameters are selected optically using flow cytometry and subjected to next-generation sequencing. Using PMF-seq, we recover genes differentially required for mitochondrial respiratory chain branching and reversibility. We demonstrate that human D-lactate dehydrogenase specifically conveys electrons from D-lactate into cytochrome c to support mitochondrial membrane polarization. Finally, we screen for genetic modifiers of tBID, a pro-apoptotic protein that acts directly and acutely on mitochondria. We find the loss of the complex V assembly factor ATPAF2 acts as a genetic sensitizer of tBID's acute action. We anticipate that PMF-seq will be valuable for defining genes critical to the physiology of mitochondria and other organelles. - Source: PubMed
Publication date: 2024/02/27
To Tsz-LeungMcCoy Jason GOstriker Naomi KSandler Lev SMannella Carmen AMootha Vamsi K - This review aims to report all the recent studies that are implicated in DNA methylation analysis in the field of allergy and to underline the complexity of the study methodologies and results. - Source: PubMed
Publication date: 2023/01/25
Legaki EvangeliaTaka StylianiPapadopoulos Nikolaos G - Recent development of deep-learning methods has led to a breakthrough in the prediction accuracy of 3D protein structures. Extending these methods to protein pairs is expected to allow large-scale detection of protein-protein interactions (PPIs) and modeling protein complexes at the proteome level. - Source: PubMed
Pei JiminZhang JingCong Qian - The study of epigenetics has improved our understanding of mechanisms underpinning gene-environment interactions and is providing new insights in the pathophysiology of respiratory allergic diseases. We reviewed the literature on DNA methylation patterns across different tissues in asthma and/or rhinitis and attempted to elucidate differentially methylated loci that could be used to characterize asthma or rhinitis. Although nasal and bronchial epithelia are similar in their histological structure and cellular composition, genetic and epigenetic regulation may differ across tissues. Advanced methods have enabled comprehensive, high-throughput methylation profiling of different tissues (bronchial or nasal epithelial cells, whole blood or isolated mononuclear cells), in subjects with respiratory conditions, aiming to elucidate gene regulation mechanisms and identify new biomarkers. Several genes and CpGs have been suggested as asthma biomarkers, though research on allergic rhinitis is still lacking. The most common differentially methylated loci presented in both blood and nasal samples are ACOT7, EPX, KCNH2, SIGLEC8, TNIK, FOXP1, ATPAF2, ZNF862, ADORA3, ARID3A, IL5RA, METRNL and ZFPM1. Overall, there is substantial variation among studies, (i.e. sample sizes, age groups and disease phenotype). Greater variability of analysis method detailed phenotypic characterization and age stratification should be taken into account in future studies. - Source: PubMed
Legaki EvangeliaArsenis ChristosTaka StylianiPapadopoulos Nikolaos G - The plateau adaptability and stress resistance of yaks are widely known based on their capacity to survive under severe habitat conditions. However, a few studies on brain mitochondria have characterized these adaptations at the protein level. We identified and quantified the brain mitochondrial proteins using isobaric tags for relative and absolute quantification (iTRAQ) and Proteomics. Western blotting was used to verify changes in the expression of target proteins. A total of 57 differentially abundant proteins (DAPs) were identified in the yak brain tissue. Gene Ontology (GO) analysis showed molecular functions of these DAPs including downregulated oxidoreductase activity but upregulated coenzyme binding. Significantly enriched biological processes were oxidation-reduction process (downregulated) and small molecule metabolic processes (upregulated). STRING protein interaction analysis indicated a complex interaction between dehydrogenase, transaminase, and ATP synthetase families. Reactome pathway analysis highlighted that the majority of DAPs participated in aerobic metabolic pathways such as metabolism, citric acid cycle, and respiratory electron transport. Immunoblotting confirmed that changes in FKBP4 and ATPAF2 expression were consistent with the results of mass spectrometry. We performed a high-throughput screening to identify DAPs in brain mitochondria between yak and cattle, which could explain the plateau adaptability of yaks. - Source: PubMed
Publication date: 2021/08/31
Ma XiaomingZhang QiangLa YongfuFu DonghaiJiang HiuBao PengjiaWu XiaoyunChu MinGuo XianYan PingLiang Chunnian