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Human Polyclonal DNM2 Primary Antibody for WB - ABIN152770
McNiven: Dynamin: a molecular motor with pinchase action. in Cell 1998
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Human Monoclonal DNM2 Primary Antibody for IHC, ELISA - ABIN966018
Quan, Robinson: Rapid purification of native dynamin I and colorimetric GTPase assay. in Methods in enzymology 2006
Show all 2 Pubmed References
Human Monoclonal DNM2 Primary Antibody for IHC (fro), IHC (p) - ABIN3073353
Yoo, Jeong, Kwon, Hur, Park, Han: Activation of dynamin I gene expression by Sp1 and Sp3 is required for neuronal differentiation of N1E-115 cells. in The Journal of biological chemistry 2002
Show all 2 Pubmed References
It has been found that Dyn2 is more efficiently recruited to clathrin-coated pits (CCPs) than Dyn1, and that Dyn2 but not Dyn1 exhibits a pronounced burst of assembly, presumably into supramolecular collar-like structures that drive membrane scission and clathrin-coated vesicle (CCV) formation.
We propose a model where upon autophagy induction, SNX18 recruits Dynamin-2 to induce budding of ATG9A and ATG16L1 containing membranes from recycling endosomes that traffic to sites of autophagosome formation.
Our findings also support a model in which impairment of actin-dependent trafficking contributes to the pathological mechanism in dynamin-2-associated CNM.
This study showed the centronuclear myopathies with mutation in DNM2.
DNM2 is a substrate for CDK1-dependent phosphorylation, which plays an important role in the regulation of human sperm acrosomal exocytosis.
Data found DNM2 highly expressed compared in both forms of ALL and associated with poor prognosis and with tumor cell proliferation. Also, Ikaros directly binds the DNM2 promoter and suppresses its expression.
Inhibition of cortactin or dynamin-2 abrogated the increased virus entry observed in DBN1-deficient cells, suggesting that DBN1 suppresses dynamin-mediated endocytosis via interaction with cortactin.
a new AHI-1-BCR-ABL-DNM2 protein complex was uncovered, which regulates leukemic properties of these cells through a unique mechanism of cellular endocytosis and ROS-mediated autophagy. Thus, targeting this complex may facilitate eradication of LSCs for curative therapies
dynamin-2, as a tetramer, might help to establish hemi-fusion and stabilizes the pore during HIV-1 fusion.
Data suggest DNM2/RRAGB- (or DNM2/RRAGC-)dependent endocytosis of extracellular amino acids (AAs) plays critical role in mTORC1 transport/activation; recruitment of mTORC1 from cytoplasm to lysosome is suppressed by DNM2 inhibition; AA deprivation appears to be main cause of mTORC1 inactivation via DNM2 inhibition. (RHEB = Ras homolog enriched in brain; DNM2 = dynamin II; RRAG = Ras-related GTP binding protein)
We demonstrate that the dynamin2 effect on T cell adhesion does not involve integrin affinity regulation but instead relies on its ability to modulate integrin valency.
Thus, dynamin2 contributes to bladder cancer invasion by controlling invadopodia formation in bladder cancer cells and may prove a valuable therapeutic target.
Study showed that dynamin 2 and cortactin participate in the formation of F-actin bundles, which stabilize filopodia in migrating cancer cells.
Data demonstrate that dynamin II is required for the E2:ERalpha signaling of physiological functions and uncovers a role for autophagy in the control of ERalpha turnover.
This study reported the clinical characteristics, molecular diagnosis strategy, and DNM2 gene mutations of four Chinese Han patients with centronuclear myopathy.
Results demonstrate that overexpression of human DNM2 mRNAs, containing different disease-related mutations, cause a continuum of pathological features in zebrafish similarly to what observed in human centronuclear myopathies and neuropathies.
uncover a link between the dynamin 2 function and JNK signaling which leads to AP-1 induction
results provide evidence for a novel Arf6 activation mechanism by Dyn2 through EFA6B and EFA6D in CME in a manner dependent upon the GTPase activity of Dyn2
We conclude that DNM2 is a novel negative regulator of NO production in mouse collecting ducts.
In marked contrast to invadopodia, this degradation does not require the action of Src kinase, Cdc42 or Dyn2. Rather, inhibition of Dyn2 causes a marked upregulation of stromal matrix degradation
these results indicate that BIN1 and DNM2 regulate muscle development and organization, function through a common pathway, and define BIN1 as a negative regulator of DNM2 in vitro and in vivo during muscle maturation.
DNM2 knockdown via two different strategies can efficiently correct the myopathy due to DNM2 mutations.
analysis of epistasis between Mtm1 and Dnm2 reveal possibilities for DNM2 knockdown as a therapeutic approach for X-linked centronuclear myopathy (XLCNM), or myotubular myopathy
Excitation-contraction coupling is impaired in the muscle fibres of the Dnm22 (R465W) mutant mice.
The authors demonstrate that ablation of DNM2 in early spermatogenesis results in germ cell arrest during prophase I of meiosis, subsequent loss of all post-meiotic germ cells and concomitant sterility. These effects become exacerbated with age, and ultimately result in the demise of the spermatogonial stem cells and a Sertoli cell only phenotype.
expressed throughout the epididymis, but localized to the Golgi apparatus of the principal cells in the proximal segment and the luminal border of these cells in more distal segments
Loss of Dynamin 2 GTPase function results in microcytic anaemia.
DNM2 mutations cooperate with Lmo2 T-cell oncogenes by enhancing IL-7 signalling.
Genetic disruption of Dyn2 GTPase activity selectively in hepatic stellate cells enhances fibrogenesis.
Oxidative stress-induced apoptosis and reactive oxygen species production are attenuated by not only Drp1 inhibition but also Dynamin 2 inhibition, implicating Dynamin 2 as a mediator of oxidative stress in cardiomyocytes.
Results show that centronuclear myopathy associated Dyn2 mutants are gain-of-function mutations, and their primary effect in muscle is T-tubule disorganization, which explains the susceptibility of muscle to Dyn2 hyperactivity.
Dynamin 2 might participate in the early embryonic development through an actin-based cytokinesis
Dynamin 2 has a role in endocytosis and in sustaining T-cell receptor signaling and driving metabolic reprogramming in T lymphocytes
DNM2-dependent endocytosis in megakaryocytes regulates megakaryopoiesis, thrombopoiesis, and bone marrow homeostasis.
Thus dynamin that was recently found to control late stages of myoblast fusion also controls late stages of macrophage fusion, revealing an intriguing conserved mechanistic motif shared by diverse cell-cell fusion processes.
Using an inducible knockout mouse model to generate dynamin 1- and 2-deficient primary osteoclast precursors and myoblasts, it was shown that fusion of both cell types requires dynamin.
FGF21 has a role in promoting endothelial cell angiogenesis through a dynamin-2 and Rab5 dependent pathway
Dynamin 2 regulates spindle migration and polar body extrusion during mouse oocyte meiosis through an actin-based pathway
Dynamin-2 directs actin polymerization at the exocytosis site where both, in concert, adjust the hormone quantal release.
role of the proline-rich domain of dynamin-2 in in vitro potentiation of endothelial nitric-oxide synthase activity.
Knocking down dynamin-2 by small interfering RNA reduced both leukotoxin internalization and cytotoxicity.
LKT-mediated cell death involve dynamin-2 and cyclophilin D
Data confirm that the zebrafish dnm2a knockdown is a valuable model for dynaminopathies.
DNM2-S619L causes disease, in part, by interfering with membrane tubulation
Our findings suggest that dnm2 and dnm2-like are orthologs to human DNM2, and that they are required for normal zebrafish development.
Upregulation of miR-124 expression corresponded to decreased expression of its target, DNM2, in the Japanese encephalitis virus -infected PK15 cells.
Dynamin 2 possibly regulates porcine oocyte maturation through its effects on actin-mediated spindle positioning and cytokinesis, and that this may depend on regulating ARP2 localization.
Dynamins represent one of the subfamilies of GTP-binding proteins. These proteins share considerable sequence similarity over the N-terminal portion of the molecule, which contains the GTPase domain. Dynamins are associated with microtubules. They have been implicated in cell processes such as endocytosis and cell motility, and in alterations of the membrane that accompany certain activities such as bone resorption by osteoclasts. Dynamins bind many proteins that bind actin and other cytoskeletal proteins. Dynamins can also self-assemble, a process that stimulates GTPase activity. Five alternatively spliced transcripts encoding different proteins have been described. Additional alternatively spliced transcripts may exist, but their full-length nature has not been determined.
, dynamin 2
, dynamin II