Polyclonal Rabbit DNM2 Antibody
- Known as:
- Polyclonal Rabbit DNM2 Antibody
- Catalog number:
- abx000741
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- Polyclonal Rabbit DNM2 Antibody
Related genes to: Polyclonal Rabbit DNM2 Antibody
- 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: Polyclonal Rabbit DNM2 Antibody
Related articles to: Polyclonal Rabbit DNM2 Antibody
- 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) PASMCs, 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 - Autophagy involves the rapid growth of phagophores through membrane addition. This growth is triggered by vesicles containing the Atg9A protein. However, Atg9A is not incorporated into mature autophagosomes. We now demonstrate that Dynamin-2 (Dnm2) colocalizes with the BAR domain protein Endophilin-B1 (EndoB1/Bif-1/SH3GLB1) and other autophagy proteins when autophagy is induced. Our data suggest that Atg9A is retrieved from phagophores via fission, with Dnm2 acting as the membrane scission protein. Blocking Atg9A recycling, either by mutating Dnm2, using RNA interference, or applying chemical inhibitors, results in Atg9A remaining in autophagosomes and being degraded during autophagy. Overall, these findings provide new insights into the roles of membrane-scission proteins in autophagy. - Source: PubMed
Publication date: 2026/03/13
Caliri AndrewRiera Alejandro MartorellSaha AkashKolitsida PanagiotaMartinez Cinta IriondoItskanov SamuelSteffen JanosKoehler Carla Mvan der Bliek Alexander M - This study aims to explore the potential molecular mechanisms by which di (2-ethylhexyl) phthalate (DEHP) exposure induces pulmonary arterial hypertension (PAH). - Source: PubMed
Publication date: 2026/03/20
Li HuaJiang YingchunLi Jijia