Alternative titles; symbols
HGNC Approved Gene Symbol: DNM2
SNOMEDCT: 763346009, 765745007;
Cytogenetic location: 19p13.2 Genomic coordinates (GRCh38) : 19:10,718,079-10,831,903 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 19p13.2 | Centronuclear myopathy 1 | 160150 | Autosomal dominant | 3 |
| Charcot-Marie-Tooth disease, axonal type 2M | 606482 | Autosomal dominant | 3 | |
| Charcot-Marie-Tooth disease, dominant intermediate B | 606482 | Autosomal dominant | 3 | |
| Lethal congenital contracture syndrome 5 | 615368 | Autosomal recessive | 3 |
DNM2 is a ubiquitously expressed large GTPase involved in clathrin (see 118955)-dependent and -independent endocytosis and intracellular membrane trafficking. DNM2 interacts tightly with actin and microtubule networks and may have a role in centrosome function (summary by Durieux et al., 2010).
Dynamins (DNMs) are members of a group of GTPases that share high homology in their N-terminal regions. Mammals have at least 3 DNMs: DNM1 (602377), DNM2, and DNM3 (611445). Diatloff-Zito et al. (1995) had previously isolated a human genomic DNA fragment by its capacity to correct the mitomycin C hypersensitivity of cells from a Fanconi anemia patient belonging to genetic complementation group D (FACD; 227646). Using this fragment, they screened a human fibroblast cDNA library and isolated a cDNA encoding DNM2. The predicted 866-amino acid protein is 73% and 98% identical to DNM1 and rat Dnm2, respectively. It contains the 3 consensus sequence elements characteristic of GTP-binding proteins at its N terminus, a pleckstrin homology (PH) domain, and a basic, proline-rich C-terminal region that contains multiple SRC homology 3 domains. DNM2 contains 9 consensus motifs for CDC2 (116940) phosphorylation, indicating a potential role at the G2/mitosis transition. Northern blot analysis detected a 3.6-kb transcript in all tissues examined, with highest expression in heart and skeletal muscle. Sequencing and RT-PCR identified alternative splicing variants of DNM2. The authors suggested that multiple rounds of duplication and divergence occurred within DNM gene evolution. No alterations in DNM2 sequence or mRNA expression were detected in the FACD patient studied.
By in situ hybridization with a Dnm2 mRNA probe, Koutsopoulos et al. (2013) found Dnm2 expression in most mouse embryonic tissues, including the peripheral nervous system, but not in skeletal muscle or heart.
Gomez et al. (2005) found that DYN2 accumulated at the T cell-antigen presenting cell (APC) interface in the presence of antigen. DYN2 knockdown experiments showed that DYN2 coupled T-cell receptor (TCR)-mediated signaling pathways to those regulating IL2 (147680) promoter activity and CD69 (107273) expression. Further experiments identified DYN2 as a critical regulator of the actin cytoskeleton in response to TCR engagement. The proline-rich domain of DYN2 interacted directly with the SH3 domain of VAV1 (164875), and this interaction was required for T-cell activation. Gomez et al. (2005) concluded that DYN2 regulates actin reorganization at the immunologic synapse and links to VAV1 and its downstream signaling pathways after TCR engagement.
Orth and McNiven (2003) found that Dyn2 associated with amphiphysin (600418) on phagosomes in cultured cells. Expression of a GTPase-deficient Dyn2 mutant prevented vesiculation and induced the formation of long plasma membrane invaginations coated with the mutant protein and terminated with a clathrin tip or bulb.
In studies in cultured mouse podocytes and rodent models of proteinuria, Sever et al. (2007) showed that during proteinuric kidney disease, induction of cytoplasmic cathepsin L (CTSL; 116880) led to cleavage of dynamin at a conserved site between amino acids 354 and 359, resulting in reorganization of the podocyte actin cytoskeleton and proteinuria. Dynamin mutants that lacked the CTSL site, or rendered the CTSL site inaccessible through dynamin self-assembly, were resistant to CTSL cleavage. When delivered into mice, these mutants restored podocyte function and resolved proteinuria. Sever et al. (2007) concluded that dynamin is a critical regulator of renal permselectivity that is specifically targeted by proteolysis under pathologic conditions.
Lee et al. (2016) reported that the ubiquitously expressed classical DYN2 is a fundamental component of the mitochondrial division machinery. A combination of live-cell and electron microscopy in 3 different mammalian cell lines revealed that DYN2 works in concert with DRP1 (603850) to orchestrate sequential constriction events that build up to division. Lee et al. (2016) concluded that their work underscores the biophysical limitations of DRP1 and positions DYN2, which has intrinsic membrane fission properties, at the final step of mitochondrial division.
Zuchner et al. (2005) determined that the DNM2 gene contains 22 exons, 20 of which are coding.
By interspecific backcross analysis, Klocke et al. (1997) found that the mouse Dnm2 gene is closely linked to the Icam1 gene (147840) on the proximal portion of chromosome 9, in a region with homologies to human 19p, 8q, and 11q. That the human ICAM1 gene is located on 19p13.3-p13.2 is evidence that the DNM2 gene is also in that region. The finding of mutations in the DNM2 gene in families with a form of autosomal dominant intermediate Charcot-Marie-Tooth disease (606482) that maps to 19p13.2-p12 is further confirmation of the mapping of DNM2 to chromosome 19.
Charcot-Marie-Tooth Disease, Dominant Intermediate B
Because the DNM2 gene maps to 19p13.2-p12 and shares domains similar to those of genes known to be involved in axonal Charcot-Marie-Tooth disease (see 118210), Zuchner et al. (2005) considered it a candidate gene for the form of dominant intermediate Charcot-Marie-Tooth disease that maps to chromosome 19p13.2-p12 (CMTDIB; 606482). They identified 3 unique mutations in the DNM2 pleckstrin homology domain in 3 unrelated families with DI-CMTB. These mutations disturbed the function of DNM2 in a cellular model. DNM2 represented the third protein mutated in CMT that contains a GTPase domain and is related to fusion or fission of cellular membranes. In 2 of the families neutropenia cosegregated with the neuropathy; these families each had a mutation affecting lys558 (602378.0002, 602378.0003), which suggested that this residue has a function in maturation or survival of peripheral blood cells.
Charcot-Marie-Tooth Disease Type 2M
In affected members of a family with autosomal dominant Charcot-Marie-Tooth Disease (CMT2M; see 606482), Fabrizi et al. (2007) identified a heterozygous missense mutation in the DNM2 gene (G533C; 602378.0008). The phenotype was milder than that reported for other CMT patients with DNM2 mutations and was more consistent with an axonal form of CMT.
Centronuclear Myopathy 1
Bitoun et al. (2005) carried out genomewide linkage mapping analysis in 2 families with autosomal dominant centronuclear myopathy (CNM1; 160150), narrowing the CNM1 locus to an 11-Mb interval on 19p13.2. The DNM2 gene, which maps to this region, was considered a good candidate. Sequencing of exons and intron-exon boundaries in the probands of 3 families identified heterozygous mutations. Two were located in exon 8 and involved the same arg369 residue, (R369Q, 602378.0004; R369W, 602378.0005), and 1 was in exon 11 and involved an R465W mutation (602378.0006). Another mutation, E368K (602378.0007), was a de novo mutation in 1 family.
Tosch et al. (2006) described a patient with centronuclear myopathy who carried heterozygous mutations in both the DNM2 (E368K; 602378.0007) and MTMR14 (Y462C; 611089.0002) genes. They noted that whereas centronuclear myopathy patients with other characterized mutations in DYN2 usually have an age of onset in childhood or adulthood, the age of onset in their patient was neonatal. The report raised the possibility of MTMR14 being a modifier of the phenotype in some cases of centronuclear myopathy.
Bitoun et al. (2007) identified 4 different de novo heterozygous DNM2 mutations (see, e.g., 602378.0010; 602378.0011) in 5 unrelated patients with sporadic CNM. All mutations were in exon 16 of the DNM2 gene within the pleckstrin homology domain. Three of the patients had a severe disorder with onset at birth.
Using in vitro sedimentation assays, Wang et al. (2010) showed that centronuclear myopathy-associated mutant DNM2 proteins (see, e.g., 602378.0005-602378.0007) formed more stable dynamin polymers in the presence of GTP compared to wildtype, presumably reflecting abnormally strong dynamin-dynamin interactions. The mutant protein aggregates were less sensitive to disassociation by GTP, and retained higher GTPase activities compared to wildtype. The observations suggested that the affected residues, such as glu368, arg369, and arg465, normally function to prevent excessive or prolonged dynamin assembly.
Lethal Congenital Contracture Syndrome 5
In 3 sibs, born of consanguineous Pakistani parents, with lethal congenital contracture syndrome-5 (LCCS5; 615368), Koutsopoulos et al. (2013) identified a homozygous missense mutation in the DNM2 gene (F379V; 602378.0013). The infants all showed severe hypotonia with lack of spontaneous movement and respiratory insufficiency at birth, resulting in death in a few days to months. Each also showed retinal hemorrhages. Studies on patient cells and in vitro functional analysis indicated that the mutation was hypomorphic. Animal studies in mice and zebrafish suggested a role for Dnm2 in the development of muscle fibers and vasculature.
By homologous recombination, Durieux et al. (2010) developed a line of mice expressing human DNM2 with the R465W substitution (602378.0006). The vast majority of homozygous mutants died during the first hours of life. Homozygous mutant muscle fibers showed multiple structural abnormalities, disorganized intermyofibrillar networks, and loss of oxidative enzyme activity. Homozygous mutant embryonic fibroblasts showed impaired clathrin-mediated endocytosis. Heterozygous R465W mice showed normal development and locomotor activity and lived as long as wildtype littermates. However, they developed atrophy of the tibialis anterior muscle at 2 months, concomitant with impaired contractile properties and development of muscle weakness, and atrophy progressed to other muscles at 8 months. DNM2-R465W protein was expressed at wildtype levels and showed normal transversal striated pattern along the I band and expression in several other muscle regions, including sarcoplasm, perinuclear region, and postsynaptic region of the neuromuscular junction. Histopathologic abnormalities mainly affected mitochondria and reticular networks. Heterozygous R465W fibers also showed increased calcium concentration and intracellular Dnm2 and dysferlin (DYSF; 603009) accumulation. A similar accumulation of DYSF was found in biopsies from centronuclear myopathy patients with mutations in the DNM2 gene.
Koutsopoulos et al. (2013) found that morpholino knockdown of Dnm2 in zebrafish embryos resulted in lethality in 10% and bent tails in 20%. Morphant muscle fibers showed mild misalignment of muscle fibers; muscular innervation appeared normal. There were also defects in the endothelium of the vascular system. The findings suggested that Dnm2 has a pleiotropic role during development.
In a North American family with dominant intermediate Charcot-Marie-Tooth disease (CMTDIB; 606482), Zuchner et al. (2005) found a 9-bp deletion of the 3-prime end of exon 14 of the DNM2 gene (1652_1659+1delATGAGGAGg). The mutation was predicted to result in 2 alternative mRNA products, one with a premature stop codon resulting from a shift of the open reading frame (D550fs) and the other an in-frame mRNA with a predicted deletion of 3 amino acids (D551_E553del) produced by disruption of the original 3-prime splice site and use of a newly introduced splice site with higher predicted splicing activity.
In an Australian family with dominant intermediate Charcot-Marie-Tooth disease (CMTDIB; 606482), Zuchner et al. (2005) found that affected individuals carried a mutation in exon 15 of the DNM2 gene, 1672A-G, resulting in the amino acid substitution lys558-to-glu (K558E). Subclinically low counts of neutrophils and, in some affected individuals, few lymphocytes, erythrocytes, and platelets cosegregated with CMT.
In a Belgian family with dominant intermediate Charcot-Marie-Tooth disease and associated neutropenia (CMTDIB; 606482), Zuchner et al. (2005) identified a deletion of nucleotides 1672 through 1674 (1672_1674delAAG) in the DNM2 gene, resulting in deletion of a single amino acid, lys558. That an abnormality of lys558 was found in 2 families (see also 602378.0002) in which neutropenia, not a general feature of dominant intermediate Charcot-Marie-Tooth disease, cosegregated with the neuropathy implied that this residue has a function in maturation or survival of peripheral blood cells. Congenital neutropenia (202700) is caused by mutations in the gene elastase-2 gene (ELA2; 130130), which maps to 19p13.3. In the Belgian family, Zuchner et al. (2005) excluded mutations in ELA2 as the cause of neutropenia by sequence analysis of all coding exons.
In a follow-up of the Belgian family reported by Zuchner et al. (2005), Claeys et al. (2009) found that 1 mutation carrier had neutropenia and cataracts without signs of a neuropathy. In addition, 5 members of this family had early-onset cataracts in their teenage years.
In 14 members of a family from French Guyana with autosomal dominant centronuclear myopathy (CNM1; 160150), Bitoun et al. (2005) identified a heterozygous 1106G-A mutation in exon 8 of the DNM2 gene, resulting in an arg369-to-gln (R369Q) substitution.
In affected members of a French family with autosomal dominant centronuclear myopathy (CNM1; 160150), Bitoun et al. (2005) identified a heterozygous 1105C-to-T transition in exon 8 of the DNM2 gene that resulted in an arg369-to-trp (R369W) substitution.
In affected members of a French family with autosomal dominant centronuclear myopathy (CNM1; 160150), Bitoun et al. (2005) identified a heterozygous 1393C-T transition in exon 11 of the DNM2 gene, resulting in an arg465-to-trp (R465W) substitution. This mutation was found in 5 additional families with CNM1, 2 Belgian, 1 German, 1 from Great Britain, and 1 from the United States.
In a French proband with centronuclear myopathy (CNM1; 160150), Bitoun et al. (2005) identified a heterozygous 1102G-to-A transition in exon 8 of the DNM2 gene that resulted in a glu368-to-lys (E368K) substitution. The mutation occurred de novo.
Tosch et al. (2006) reported this mutation in heterozygosity in a 36-year-old woman with centronuclear myopathy who presented with neonatal hypotonia, muscle weakness, and ophthalmoparesis. She also carried a heterozygous missense mutation in the myotubularin-related protein-14 gene (MTMR14; 611089.0002). Both mutations occurred de novo. The report raised the possibility of MTMR14 being a modifier of the phenotype in some cases of centronuclear myopathy.
In affected members of a family with autosomal dominant axonal Charcot-Marie-Tooth disease type 2M (CMT2M; see 606482), Fabrizi et al. (2007) identified a heterozygous 1597G-T transversion in the DNM2 gene, resulting in a gly533-to-cys (G533C) substitution. The phenotype was milder than that reported for other CMT patients with DNM2 mutations and was more consistent with an axonal form of CMT.
In a 45-year-old proband of a family with autosomal dominant axonal Charcot-Marie-Tooth disease type 2M (CMT2M; see 606482), Fabrizi et al. (2007) identified a heterozygous 1697T-A transversion in the DNM2 gene, resulting in a leu566-to-his (L566H) substitution. The phenotype was milder than that reported for other CMT patients with DNM2 mutations and was more consistent with an axonal form of CMT.
In 2 unrelated patients with sporadic centronuclear myopathy (CNM1; 160150), Bitoun et al. (2007) identified a de novo heterozygous 1856C-T transition in exon 16 of the DNM2 gene, resulting in a ser619-to-leu (S619L) substitution within the pleckstrin homology domain. Both patients had a severe phenotype, with onset at birth necessitating ventilation and nasogastric feeding, and delayed motor development. Another unrelated patient with a milder phenotype had a different heterozygous mutation in the same codon (S619W; 602378.0011).
In a patient with sporadic centronuclear myopathy (CNM1; 160150), Bitoun et al. (2007) identified a de novo heterozygous 1856C-G transversion in exon 16 of the DNM2 gene, resulting in a ser619-to-trp (S619W) substitution. Two other unrelated patients with a more severe phenotype had a different heterozygous mutation in the same codon (S619L; 602378.0010).
In a mother and her 2 adult daughters with autosomal dominant axonal Charcot-Marie-Tooth disease type 2M (CMT2M; see 606482), Gallardo et al. (2008) identified a heterozygous 1072G-A transition in exon 7 of the DNM2 gene, resulting in a gly358-to-arg (G358R) substitution in a highly conserved region in the middle domain. The patients were ages 55, 32, and 23, and motor nerve conduction velocities were 33, 46, and 50 m/s, respectively. All had progressive gait unsteadiness and foot deformities, including pes cavus and toe clawing, in the first decade of life. All had distal muscle weakness and atrophy of the lower limbs, and the mother also had hand weakness and atrophy. Ankle reflexes were absent in all 3, and all had hypoesthesia of the lower limbs. MRI studies showed fatty infiltration of the calf muscles, particularly in the anterior compartment. The fatty infiltration increased distally and was massive in the foot musculature. Muscle edema was also present in affected muscles. In a follow-up of the family reported by Gallardo et al. (2008), Claeys et al. (2009) stated that the phenotype was consistent with axonal CMT2.
In 3 sibs, born of consanguineous Pakistani parents, with lethal congenital contracture syndrome-5 (LCCS5; 615368), Koutsopoulos et al. (2013) identified a homozygous c.1135T-G transversion in exon 9 of the DNM2 gene, resulting in a phe379-to-val (F379V) substitution at a highly conserved residue in the middle domain of the protein. The mutation, which was found by homozygosity mapping followed by candidate gene sequencing, was not present in 100 Pakistani controls and was absent from SNP databases. Patient fibroblasts showed a 20% reduction in DNM2-dependent endocytosis, and recombinant F379V DNM2 showed a 20% reduction in GTPase activity, consistent with its being a hypomorphic allele. The patients showed decreased fetal movements and severe hypotonia with respiratory insufficiency at birth. They had areflexia, lack of spontaneous movement, joint contractures, and thin ribs and bones. In addition, all had retinal hemorrhages and 2 had evidence of intracranial bleeding (subdural hematoma and blood in the subarachnoid cavity). Muscle biopsy of 1 patient showed small rounded fibers with some centralized nuclei, suggestive of a congenital myopathy component, whereas muscle biopsy of another patient showed atrophic fibers without obvious centralization of nuclei. EMG studies of 1 patient suggested a myopathy or lower motor neuron disease, whereas in the other 2 patients, EMG revealed low nerve conduction velocities, suggesting a hypomyelinating neuropathy or anterior horn disease. Death occurred at ages 5 days, 19 days, and 4 months. Both parents showed decreased reflexes on examination, and skeletal muscle biopsy of the mother showed fiber size variation and centralized nuclei, suggestive of a mild form of centronuclear myopathy.
Bitoun, M., Bevilacqua, J. A., Prudhon, B., Maugenre, S., Taratuto, A. L., Monges, S., Lubieniecki, F., Cances, C., Uro-Coste, E., Mayer, M., Fardeau, M., Romero, N. B., Guicheney, P. Dynamin 2 mutations cause sporadic centronuclear myopathy with neonatal onset. Ann. Neurol. 62: 666-670, 2007. [PubMed: 17932957] [Full Text: https://doi.org/10.1002/ana.21235]
Bitoun, M., Maugenre, S., Jeannet, P.-Y., Lacene, E., Ferrer, X., Laforet, P., Martin, J.-J., Laporte, J., Lochmuller, H., Beggs, A. H., Fardeau, M., Eymard, B., Romero, N. B., Guicheney, P. Mutations in dynamin 2 cause dominant centronuclear myopathy. Nature Genet. 37: 1207-1209, 2005. [PubMed: 16227997] [Full Text: https://doi.org/10.1038/ng1657]
Claeys, K. G., Zuchner, S., Kennerson, M., Berciano, J., Garcia, A., Verhoeven, K., Storey, E., Merory, J. R., Bienfait, H. M. E., Lammens, M., Nelis, E., Baets, J., De Vriendt, E., Berneman, Z. N., De Veuster, I., Vance, J. M., Nicholson, G., Timmerman, V., De Jonghe, P. Phenotypic spectrum of dynamin 2 mutations in Charcot-Marie-Tooth neuropathy. Brain 132: 1741-1752, 2009. [PubMed: 19502294] [Full Text: https://doi.org/10.1093/brain/awp115]
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Durieux, A.-C., Vignaud, A., Prudhon, B., Viou, M. T., Beuvin, M., Vassilopoulos, S., Fraysse, B., Ferry, A., Laine, J., Romero, N. B., Guicheney, P., Bitoun, M. A centronuclear myopathy-dynamin 2 mutation impairs skeletal muscle structure and function in mice. Hum. Molec. Genet. 19: 4820-4836, 2010. [PubMed: 20858595] [Full Text: https://doi.org/10.1093/hmg/ddq413]
Fabrizi, G. M., Ferrarini, M., Cavallaro, T., Cabrini, I., Cerini, R., Bertolasi, L., Rizzuto, N. Two novel mutations in dynamin-2 cause axonal Charcot-Marie-Tooth disease. Neurology 69: 291-295, 2007. [PubMed: 17636067] [Full Text: https://doi.org/10.1212/01.wnl.0000265820.51075.61]
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Gomez, T. S., Hamann, M. J., McCarney, S., Savoy, D. N., Lubking, C. M., Heldebrant, M. P., Labno, C. M., McKean, D. J., McNiven, M. A., Burkhardt, J. K., Billadeau, D. D. Dynamin 2 regulates T cell activation by controlling actin polymerization at the immunological synapse. Nature Immun. 6: 261-270, 2005. [PubMed: 15696170] [Full Text: https://doi.org/10.1038/ni1168]
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Koutsopoulos, O. S., Kretz, C., Weller, C. M., Roux, A., Mojzisova, H., Bohm, J., Koch, C., Toussaint, A., Heckel, E., Stemkens, D., ter Horst, S. A. J., Thibault, C., Koch, M., Mehdi, S. Q., Bijlsma, E. K., Mandel, J.-L., Vermot, J., Laporte, J. Dynamin 2 homozygous mutation in humans with a lethal congenital syndrome. Europ. J. Hum. Genet. 21: 637-642, 2013. [PubMed: 23092955] [Full Text: https://doi.org/10.1038/ejhg.2012.226]
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Sever, S., Altintas, M. M., Nankoe, S. R., Moller, C. C., Ko, D., Wei, C., Henderson, J., del Re, E. C., Hsing, L., Erickson, A., Cohen, C. D., Kretzler, M., Kerjaschki, D., Rudensky, A., Nikolic, B., Reiser, J. Proteolytic processing of dynamin by cytoplasmic cathepsin L is a mechanism for proteinuric kidney disease. J. Clin. Invest. 117: 2095-2104, 2007. [PubMed: 17671649] [Full Text: https://doi.org/10.1172/JCI32022]
Tosch, V., Rohde, H. M., Tronchere, H., Zanoteli, E., Monroy, N., Kretz, C., Dondaine, N., Payrastre, B., Mandel, J.-L., Laporte, J. A novel PtdIns3P and PtdIns(3,5)P2 phosphatase with an inactivating variant in centronuclear myopathy. Hum. Molec. Genet. 15: 3098-3106, 2006. [PubMed: 17008356] [Full Text: https://doi.org/10.1093/hmg/ddl250]
Wang, L., Barylko, B., Byers, C., Ross, J. A., Jameson, D. M., Albanesi, J. P. Dynamin 2 mutants linked to centronuclear myopathies form abnormally stable polymers. J. Biol. Chem. 285: 22753-22757, 2010. [PubMed: 20529869] [Full Text: https://doi.org/10.1074/jbc.C110.130013]
Zuchner, S., Noureddine, M., Kennerson, M., Verhoeven, K., Claeys, K., De Jonghe, P., Merory, J., Oliveira, S. A., Speer, M. C., Stenger, J. E., Walizada, G., Zhu, D., Pericak-Vance, M. A., Nicholson, G., Timmerman, V., Vance, J. M. Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease. Nature Genet. 37: 289-294, 2005. [PubMed: 15731758] [Full Text: https://doi.org/10.1038/ng1514]