Ask about this productRelated genes to: TMEM120A antibody
- Gene:
- TMEM120A NIH gene
- Name:
- transmembrane protein 120A
- Previous symbol:
- -
- Synonyms:
- TMPIT, NET29
- Chromosome:
- 7q11.23
- Locus Type:
- gene with protein product
- Date approved:
- 2007-08-01
- Date modifiied:
- 2015-09-08
Related products to: TMEM120A antibody
Related articles to: TMEM120A antibody
- The synthesis of glycerolipid is essential to prevent the toxic effects of excess fatty acids. Glycerolipids are generated by the sequential attachment of acyl-CoA to glycerol by endoplasmic reticulum (ER)-localized acyltransferases, ultimately yielding non-toxic triacylglycerol that can be stored in lipid droplets. The key acyltransferase GPAT4 associates with the CHP1 protein, but the regulation of GPAT4 remains poorly understood. Here, we have used genetic, biochemical, and imaging techniques to identify TMEM120A as GPAT4-activating protein. We show that ER-localized TMEM120A and CHP1 synergistically activate GPAT4 and promote the incorporation of medium and long chain acyl-CoA into glycerolipid. C. elegans mutants of TMEM120A or CHP1 ortholog are susceptible to high-fat diet induced sterility, in part due to their deficiency in lipid droplet expansion. In mammalian cells, fatty acid supplementation and myristoylated CHP1 enhance the association of TMEM120A with GPAT4. Together, our results reveal an unexpected mechanism that alleviates lipotoxicity. - Source: PubMed
Publication date: 2026/05/07
Li YanHuang SiweiChan Lam ShingLi XuesongTo Ning-SumZhao XueJung KwangsekYang XingyuTse Yu ChungXu NingyiXia YuCheung Tom HQu JiananMak Ho Yi - Chronic pain remains a pervasive and debilitating condition with few effective treatments available. Emerging evidence reveals that transmembrane (TMEM) proteins are not merely passive structural elements but dynamic regulators of nociceptive signaling. Key TMEM family members, including TMEM100, TMEM16A/F, TMEM175, TMEM97, TMEM120A/TACAN, and TMEM233, orchestrate pain transmission by modulating ion channels, inflammatory mediators, and intracellular signaling cascades across peripheral and central pathways. Decoding their structural and functional diversity reveals new opportunities to design targeted analgesics that disrupt pathological pain at its source while sparing central nervous system side effects. By harnessing the therapeutic potential of TMEM proteins, we may redefine strategies for managing chronic and treatment-resistant pain, ultimately improving outcomes for millions affected worldwide. - Source: PubMed
Publication date: 2026/04/10
Kappara DeepikaVerma NiveditaTiwari Vinod - Efficient fatty acid (FA) re-esterification is essential for lipid homeostasis in adipocytes, yet the mechanisms coordinating Coenzyme A (CoA) availability at the endoplasmic reticulum (ER)-a major site of lipid synthesis-remain unclear. Here, we identify TMEM120A as an ER-resident CoA-binding protein that regulates intracellular FA metabolism. TMEM120A interacts with the ER-localized acyl-CoA synthetase ACSL1 and ACSL3 to promote long-chain acyl-CoA synthesis and channeling into the ER, thereby facilitating FA re-esterification and lipid cycling during lipolysis. By relieving acyl-CoA-mediated feedback inhibition of lipolysis, TMEM120A enhances lipid turnover while protecting against ER stress and lipotoxicity. Adipocyte-specific deletion of Tmem120a in mice impairs lipolysis-induced energy expenditure and exacerbates inflammation and metabolic dysfunction under high-fat diet conditions. These findings establish TMEM120A as a critical regulator of ER CoA handling and lipid flux, revealing a previously unrecognized mechanism that links intracellular CoA dynamics to systemic energy balance and metabolic health. - Source: PubMed
Publication date: 2025/12/21
Cho Yoon KeunLee JunhyuckJeong Yujin LShim MinkiMai Xuan LinhSeomoon ChangJung Cheol WoonChoi Yoon HaNamgoong SikJung Young-SukKwon Sung WonLee JuyongSeong Je KyungPark SunghyoukMottillo Emilio PGranneman James GLee Dong-KyuKim Jong KyoungLee Yun-Hee - Obesity remains a growing and global public health burden across a broad spectrum of metabolic, systemic, and neurodegenerative diseases. Previously considered merely a fat storage depot, adipose tissue is now recognized as an active endocrine organ crucial for the metabolic and systemic regulation of local and distant organs. A burgeoning line of investigation centers on adipose-derived extracellular vesicles (ADEVs) and their pivotal role in obesity-associated pathobiology. However, robust methodologies for specifically isolating and characterizing human ADEVs are lacking. To bridge this gap, we developed a robust multiparametric framework incorporating bulk and single EV characterization, proteomics, and mRNA phenotyping. EVs from matched human visceral adipose tissue, mature adipocyte-conditioned media, and plasma collected from the same bariatric surgical patients were analyzed and subjected to bottom-up proteomics analysis. This framework integrates bulk EV proteomics for cell-specific marker identification and subsequent single EV interrogation with single-particle interferometric reflectance imaging (SP-IRIS) and total internal reflection fluorescence (TIRF) microscopy. Our proteomics analysis revealed 76 unique proteins from adipose tissue-derived EVs (ATEVs), 512 unique proteins from adipocyte EVs (aEVs), and 1003 shared proteins. Prominent pathways enriched in ATEVs included lipid metabolism, extracellular matrix organization, and immune modulation, while aEVs were enriched in chromatin remodeling, oxidative stress responses, and metabolic regulation pathways. Notably, we identified obesity-associated and adipose-specific proteins, such as TMEM120A and SACM1L, highly enriched in ATEVs, and histone variants, including MACROH2A1, H3-3A, H2AC20, H2BC12, and H3-7, uniquely upregulated in aEVs. Additionally, classical adipose-associated proteins such as adiponectin and perilipin were highly enriched in ADEVs and were confirmed in circulating plasma EVs. Colocalization of key EV and adipocyte markers, including CD63 and PPARG, was validated in circulating plasma EVs. In summary, our study paves the way toward a tissue and cell-specific, multiparametric framework for an 'adiposity EV signature' in obesity-driven diseases. - Source: PubMed
Publication date: 2025/10/23
Hade Mangesh DattuGreenwald JacelynLoreto Palacio PaolaNguyen Kim TrucShantaram DhartiButsch Bradley LKim YongseokNoria SabrenaBrethauer Stacy ANeedleman Bradley JHsueh Willa AWysocki Vicki HReátegui EduardoMagaña Setty M - The main goal of this study was to pinpoint functional candidate genes associated with multiple economically important traits in Nellore cattle. After quality control, 1830 genomic regions sourced from 52 scientific peer-reviewed publications were used in this study. From these, a total of 8569 positional candidate genes were annotated for reproduction, 11,195 for carcass, 5239 for growth, and 3483 for morphological traits, and used in an over-representation analysis. The significant genes (adjusted -values < 0.05) identified in the over-representation analysis underwent prioritization analyses, and enrichment analysis of the prioritized over-represented candidate genes was performed. The prioritized candidate genes were , , , , , and for reproduction; , , , , , , , , , and for the carcass; and for growth traits; and no genes were prioritized for morphological traits. The functional analysis pinpointed the following genes: (plays a crucial role in spindle organization, which is essential in forming a robust mitotic centrosome), (involved in muscle cell differentiation), and (involved in protein deubiquitination, thereby improving growth). The enrichment of the functional candidate genes identified in this study highlights that these genes play an important role in the expression of reproduction, carcass, and growth traits in Nellore cattle. - Source: PubMed
Publication date: 2024/08/27
Ogunbawo Adebisi RMulim Henrique ACampos Gabriel SOliveira Hinayah R