FAM82C Blocking Peptide
- Known as:
- FAM82C Blocking Peptide
- Catalog number:
- 33r-5411
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- FAM82C Blocking Peptide
Related genes to: FAM82C Blocking Peptide
- Gene:
- RMDN3 NIH gene
- Name:
- regulator of microtubule dynamics 3
- Previous symbol:
- FAM82C, FAM82A2
- Synonyms:
- FLJ10579, PTPIP51, RMD3
- Chromosome:
- 15q15.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-07-27
- Date modifiied:
- 2019-03-14
Related products to: FAM82C Blocking Peptide
Related articles to: FAM82C Blocking Peptide
- Frailty, a clinical state of increased vulnerability to stressors with aging, imposes significant strain on healthcare systems. Its genetic underpinnings remain incompletely explored, highlighting the need to identify novel therapeutic targets for aging. - Source: PubMed
Publication date: 2026/04/01
Zhong JiaYuYuan MingHaoZhou EnHu Shuo - Signaling between the endoplasmic reticulum (ER) and mitochondria regulates many of the seemingly disparate physiological functions that are damaged in neurodegenerative diseases such as Alzheimer's disease, Parkinson's disease, frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS). A number of studies have now demonstrated that ER-mitochondria signaling is perturbed in these diseases and there is evidence that this may be a driving mechanism in disease onset and progression. VAPB and PTPIP51 are ER-mitochondria tethering proteins; VAPB is an ER protein and PTPIP51 is an outer mitochondrial membrane protein and the two proteins interact to enable inter-organelle signaling. The VAPB-PTPIP51 interaction is disrupted in Alzheimer's disease, Parkinson's disease, FTD and ALS. Here we review the roles of VAPB and PTPIP51 in ER-mitochondria signaling and the mechanisms by which neurodegenerative disease insults may disrupt the VAPB-PTPIP51 interaction. - Source: PubMed
Publication date: 2025/03/05
Blair KerryMartinez-Serra RaquelGosset PhilippeMartín-Guerrero Sandra MMórotz Gábor MAtherton JosephMitchell Jacqueline CMarkovinovic AndreaMiller Christopher C J - Recent genome-wide association studies (GWAS) have identified new susceptibility loci for melanoma, but their associations with multiple primary melanoma (MPM) are unclear. - Source: PubMed
Gibbs David CSmall Brittany MAutuori IsidoraLeong Siok FAli EmilyKenney JessicaLuo LiKanetsky Peter ABusam Klaus JCust Anne EAnton-Culver HodaGallagher Richard PZanetti RobertoRosso StefanoSacchetto LidiaEdmiston Sharon NConway KathleenOllila David WBegg Colin BBerwick MarianneOrlow IreneThomas Nancy E - The proximal domains of mitochondria and the endoplasmic reticulum (ER) are linked by tethering factors on each membrane, allowing the efficient transport of substances, including lipids and calcium, between them. However, little is known about the regulation and function of mitochondria-ER contacts (MERCs) dynamics under mitochondrial damage. In this study, we apply NanoBiT technology to develop the MERBiT system, which enables the measurement of reversible MERCs formation in living cells. Analysis using this system suggests that induction of mitochondrial ROS increases MERCs formation via RMDN3 (also known as PTPIP51)-VAPB tethering driven by RMDN3 phosphorylation. Disruption of this tethering caused lipid radical accumulation in mitochondria, leading to cell death. The lipid radical transfer activity of the TPR domain in RMDN3, as revealed by an in vitro liposome assay, suggests that RMDN3 transfers lipid radicals from mitochondria to the ER. Our findings suggest a potential role for MERCs in cell survival strategy by facilitating the removal of mitochondrial lipid radicals under mitochondrial damage. - Source: PubMed
Publication date: 2025/02/10
Shiiba IsshinIto NaokiOshio HijiriIshikawa YutoNagao TakahiroShimura HirokiOh Kyu-WanTakasaki EikiYamaguchi FuyaKonagaya RyoanKadowaki HisaeNishitoh HidekiTanzawa TakehitoNagashima ShunSugiura AyumuFujikawa YuutaUmezawa KeitaroTamura YasushiIl Lee ByungHirabayashi YusukeOkazaki YasushiSawa TomohiroInatome RyokoYanagi Shigeru - Aging is a gradual and irreversible natural process. With aging, the body experiences a functional decline, and the effects amplify the vulnerability to a range of age-related diseases, including neurodegenerative, cardiovascular, and metabolic diseases. Within the aging process, the morphology and function of mitochondria and the endoplasmic reticulum (ER) undergo alterations, particularly in the structure connecting these organelles known as mitochondria-associated membranes (MAMs). MAMs serve as vital intracellular signaling hubs, facilitating communication between the ER and mitochondria when regulating various cellular events, including calcium homeostasis, lipid metabolism, mitochondrial function, and apoptosis. The formation of MAMs is partly dependent on the interaction between the vesicle-associated membrane protein-associated protein-B (VAPB) and protein tyrosine phosphatase-interacting protein-51 (PTPIP51). Accumulating evidence has begun to elucidate the pivotal role of the VAPB-PTPIP51 tether in the initiation and progression of age-related diseases. In this study, we delineate the intricate structure and multifunctional role of the VAPB-PTPIP51 tether and discuss its profound implications in aging-associated diseases. Moreover, we provide a comprehensive overview of potential therapeutic interventions and pharmacological agents targeting the VAPB-PTPIP51-mediated MAMs, thereby offering a glimmer of hope in mitigating aging processes and treating age-related disorders. - Source: PubMed
Publication date: 2024/05/06
Jiang TaoRuan NanLuo PengchengWang QianWei XiuxianLi YiDai YueLin LiLv JiagaoLiu YuZhang Cuntai