Human Dynamin 2 ELISA , DNM2
- Known as:
- Human Dynamin 2 Enzyme-linked immunosorbent assay test , DNM2
- Catalog number:
- E01D0248
- Product Quantity:
- 96 Tests/kit
- Category:
- -
- Supplier:
- BGene
- Gene target:
- Human Dynamin 2 ELISA DNM2
Related genes to: Human Dynamin 2 ELISA , DNM2
- Gene:
- DNM2 NIH gene
- Name:
- dynamin 2
- Previous symbol:
- -
- Synonyms:
- DYNII, DYN2, CMTDIB, CMTDI1, DI-CMTB, CMT2M
- Chromosome:
- 19p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1996-10-11
- Date modifiied:
- 2019-04-23
Related products to: Human Dynamin 2 ELISA , DNM2
Related articles to: Human Dynamin 2 ELISA , DNM2
- Disruption of lysosomal homeostasis and accumulation of dysfunctional mitochondria contribute to degenerative pathologies including age-related macular degeneration (AMD). Here, we investigated how inhibition of autophagic lysosome reformation (ALR) alters lysosomal dynamics, mitophagy, and downstream stress signaling in retinal pigment epithelial (RPE) cells, and whether these changes are pharmacologically reversible. In ARPE-19 cells, ALR inhibition by nocodazole or siRNA-mediated depletion of kinesin-1 (UKHC) and dynamin-2 (DNM2) induced enlarged lysosomes with reduced degradative capacity, impaired mitophagic turnover, and accumulation of dysfunctional mitochondria. ALR blockade increased reactive oxygen species (ROS) and cytosolic Ca, promoted activation and mitochondrial translocation of protein kinase C (PKC), and triggered phosphorylation of glycogen synthase kinase-3β with subsequent stabilization of SNAIL, consistent with epithelial-to-mesenchymal transition (EMT). Metformin restored lysosomal homeostasis by activating AMPK and enhancing transcription factor EB (TFEB)-dependent lysosome biogenesis, thereby improving autophagic flux, limiting ROS/Ca accumulation, suppressing PKC activation, and attenuating EMT-associated marker changes. In a sodium iodate-induced oxidative injury model, metformin preserved RPE microtubule architecture and reduced lysosomal and mitochondrial abnormalities. Although these findings rely on a prolonged monolayer culture system and an acute injury model, they support a protective role for AMPK-TFEB-driven lysosome restoration in RPE stress resilience and suggest lysosome-directed repurposing potential for metformin in degenerative retinal disease. - Source: PubMed
Publication date: 2026/06/11
Son SuminKim YoonhaJang Kyoung-JinKim Dong-Eun - Centronuclear myopathy (CNM) is a genetically heterogenous congenital myopathy traditionally classified as a membrane remodeling disorder. Emerging evidence reveals that centronuclear myopathy mutations converge upon common cellular dysfunction extending beyond membrane trafficking. This review proposes a unified model positioning CNM as a disorder of impaired organelle communication and structural crosstalk. We focus on how mutations in Myotubularin1 () and gain-of-function mutations in Dynamin 2 () disrupt the triad architecture, leading to aberrant calcium handling, mitochondrial dysfunction, imbalanced reactive oxygen species (ROS) production, and defective autophagy. These dysfunctions are not isolated but form a pathological feedback loop that compromises muscle integrity and regeneration. By identifying shared mechanisms across CNM types, this review positions the disorder as the convergence of organelle stress and cytoskeletal network failure. This perspective reveals novel therapeutic strategies based on the principle that targeting a central pathological node may alleviate systemic dysfunction. However, given the complexity of the organelle feedback loop, a comprehensive, multi-target approach may ultimately be required to achieve full phenotypic rescue across all affected tissues. - Source: PubMed
Publication date: 2026/05/08
Abolibdeh BanaWilliams Charles H - Centronuclear myopathies (CNMs) are rare congenital disorders characterized by muscle weakness, fiber hypotrophy, and organelle mislocalization. Most cases arise from mutations in MTM1 or DNM2, encoding myotubularin and dynamin-2, respectively. DNM2 is a GTPase that binds lipids, oligomerizes around membranes, and mediates fission. We previously showed that DNM2 levels are elevated in MTM1-CNM patients and Mtm1-/y mice, and that normalizing DNM2 rescues disease phenotypes. However, the specific DNM2 functions driving pathology remain unclear. Here, we expressed AAV-delivered WT and DNM2 mutants in WT and Mtm1-/y mouse muscles to disrupt specific DNM2 molecular functions. In WT mice, overexpression of WT DNM2 and most mutants induced CNM-like phenotypes, including reduced force, fiber hypotrophy, and centralized nuclei, consistent with gain-of-function mechanisms. The lipid-binding-defective mutant K562E did not induce disease-like phenotype. In Mtm1-/y mice, K562E mutant markedly improved muscle force, mass, and fiber size, while others failed to rescue. Therefore, we generated Mtm1-/y Dnm2K562E/+ mice, which showed full rescue of survival, motor function, and muscle force, with improved muscle mass, fiber size, and organelle positioning despite persistently elevated DNM2 levels. This study reveals that DNM2 lipid binding, not protein abundance or GTPase activity, drives pathology, and represents the most rational therapeutic target for DNM2 therapy in MTM1-CNM. - Source: PubMed
Publication date: 2026/05/08
Gómez-Oca RaquelMassana-Muñoz XèniaReiss DavidDe Carvalho Neves JulianaDiedhiou NadegeSilva-Rojas RobertoCowling Belinda SGoret MarieLaporte Jocelyn - DRP1 (dynamin-related protein 1) mediates mitochondrial fission and permits rapid cell cycle progression in hyperproliferative cells by coordinating nuclear and mitochondrial division, a process called mitotic fission. However, DRP1 alone appears insufficient to complete fission, and the link between fission and cell cycle progression is unknown. We hypothesize that DNM2 (dynamin 2) interacts with DRP1 to complete mitochondrial fission and regulate cell cycle progression. We show that DNM2 is upregulated in pulmonary artery smooth muscle cells (PASMCs) in human and rodent pulmonary arterial hypertension (PAH), contributing to disease pathophysiology. - Source: PubMed
Publication date: 2026/04/28
Dasgupta AsishChen Kuang-HueihWu DanchenYerramilli V SiddarthaLima Patricia D AMartin Ashley YBentley Rachel E TOtt Benjamin PNandani TanviMewburn Jeffrey DTian LianAl-Qazazi RuaaEmon Isaac MColpman PierceJefferson LindsayNoordhof CurtisJones OliverHindmarch Charles C TArcher Stephen L - Sleep is thought to be important for the clearance of brain waste, but exactly how it does so is still debated. Here, we demonstrate that endocytosis in brain endothelial cells (BECs) of the blood-brain barrier (BBB) is enhanced during sleep, facilitating the removal of brain-derived waste, including amyloid-β, into the circulation. Using proteomics, in vivo tracer imaging, and endothelial-specific genetic perturbations in mice, we demonstrate that sleep enhances endocytic vesicle formation and cargo transcytosis in brain endothelial cells (BECs). Conversely, blocking endocytosis through endothelial Dnm2 knockout suppresses BEC-mediated transport and elevates sleep need, revealing a causal feedback loop between sleep and vascular endocytosis. These findings identify BBB endocytosis as a key sleep-dependent clearance pathway with implications for neurodegenerative disease. - Source: PubMed
Publication date: 2026/04/03
Li FuChen DechunSehgal Amita