Alternative titles; symbols
HGNC Approved Gene Symbol: DCTN1
SNOMEDCT: 699184009;
Cytogenetic location: 2p13.1 Genomic coordinates (GRCh38): 2:74,361,155-74,391,866 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 2p13.1 | {Amyotrophic lateral sclerosis, susceptibility to} | 105400 | Autosomal dominant; Autosomal recessive | 3 |
| Neuronopathy, distal hereditary motor, autosomal dominant 14 | 607641 | Autosomal dominant | 3 | |
| Perry syndrome | 168605 | Autosomal dominant | 3 |
The DCTN1 gene encodes p150(Glued), the largest polypeptide of the dynactin complex, which binds directly to microtubules and to cytoplasmic dynein (DYNC1H1; 600112), a microtubule-based biologic motor protein (Holzbaur and Tokito, 1996).
Holzbaur and Tokito (1996) noted that dyneins were initially discovered as enzymes that couple ATP hydrolysis to provide a force for cellular motility in eukaryotic cilia and flagella. A distinct cytoplasmic form of dynein was subsequently characterized and thought to be responsible for the intracellular retrograde motility of vesicles and organelles along microtubules (Holzbaur and Vallee, 1994). A large macromolecular complex, dynactin, is required for the cytoplasmic dynein-driven movement of organelles along microtubules. Dynactin is composed of 10 distinct polypeptides of 150, 135, 62, 50 (DCTN2; 607376), 45, 42, 37, 32, 27, and 24 kD, with a combined mass of 10 million daltons. The binding of dynactin to dynein is critical for neuronal function, as antibodies that specifically disrupt this binding block vesicle motility along microtubules in extruded squid axoplasm. Holzbaur and Tokito (1996) stated that the dynein-dynactin interaction is probably a key component of the mechanism of axonal transport of vesicles and organelles. Further evidence for a critical role for dynactin in vivo comes from the analysis of mutations in the homologous gene in Drosophila. Mutant alleles of the 'glued' gene induced disruption of the neurons of the optic lobe and compound eye in heterozygotes; null mutations are lethal.
Holzbaur and Tokito (1996) isolated and characterized cDNA clones encoding human p150(Glued), as well as alternatively spliced isoforms. Using these to isolate genomic clones, they found by genomic Southern blots that there is a single gene in the human, as had previously been observed in rat and chick.
Jang et al. (1997) cloned and characterized mouse Dctn1. The mouse protein shares 95% amino acid identity with the human protein. The authors found no abnormalities of the gene in mnd2 mice.
Eaton et al. (2002) disrupted the dynactin complex in Drosophila, using 3 separate perturbations: dsRNA interference with arp1 (homolog of ACTR1A; 605143), mutation in p150/Glued, and a dominant-negative Glued transgene. In all 3 cases, the disruption resulted in an increase in the frequency and extent of synaptic retraction events at the neuromuscular junction. Eaton et al. (2002) concluded that dynactin functions locally within the presynaptic arbor to promote synapse stability at the neuromuscular junction.
Kim et al. (2004) showed that BBS4 (600374) protein localizes to the centriolar satellites of centrosomes and basal bodies of primary cilia, where it functions as an adaptor of the p150(glued) subunit of the dynein transport machinery to recruit pericentriolar material-1 protein (PCM1; 600299) and its associated cargo to the satellites. Silencing of BBS4 induces PCM1 mislocalization and concomitant deanchoring of centrosomal microtubules, arrest in cell division, and apoptotic cell death.
Gauthier et al. (2004) showed that huntingtin (613004) specifically enhances vesicular transport of brain-derived neurotrophic factor (BDNF; 113505) along microtubules. They determined that huntingtin-mediated transport involves huntingtin-associated protein-1 (HAP1; 600947) and the p150(Glued) subunit of dynactin, an essential component of molecular motors. BDNF transport was attenuated both in the disease context and by reducing the levels of wildtype huntingtin. The alteration of the huntingtin/HAP1/p150(Glued) complex correlated with reduced association of motor proteins with microtubules. The polyglutamine-huntingtin-induced transport deficit resulted in the loss of neurotrophic support and neuronal toxicity. Gauthier et al. (2004) concluded that a key role of huntingtin is to promote BDNF transport and suggested that loss of this function might contribute to pathogenesis.
Using yeast 2-hybrid and immunoprecipitation analyses, Shimojo (2008) showed that human RILP (PRICKLE1; 608500) and huntingtin interacted directly with dynactin-1 to form a triplex. REST bound to the triplex through direct interaction with RILP, forming a quaternary complex involved in nuclear translocation of REST in non-neuronal cells. In neuronal cells, the complex also contained HAP1, which affected interaction of disease-causing mutant huntingtin, but not wildtype huntingtin, with dynactin-1 and RILP. Overexpression and knockout analyses demonstrated that the presence of HAP1 in the complex prevented nuclear translocation of REST and thereby regulated REST activity.
Using in vivo skin-specific lentiviral RNA interference, Williams et al. (2011) investigated spindle orientation regulation and provided direct evidence that LGN (609245), NuMA (164009), and dynactin are involved. In compromising asymmetric cell divisions, Williams et al. (2011) uncovered profound defects in stratification, differentiation, and barrier formation, and implicated Notch (190198) signaling as an important effector. Williams et al. (2011) concluded that asymmetric cell division components act by reorientating mitotic spindles to achieve perpendicular divisions, which in turn promote stratification and differentiation. Furthermore, the resemblance between their knockdown phenotypes and Rbpj (147183) loss-of-function mutants provided important clues that suprabasal Notch signaling is impaired when asymmetric cell divisions do not occur.
Using mouse and human constructs, Zhapparova et al. (2013) found that SLK (616563) phosphorylated a serine in the basic microtubule-binding domain of the minor p150(GLUED)1A isoform of DCTN1 and regulated dynactin centrosomal localization. This phosphorylation did not affect dynactin microtubule-organizing properties. Phosphorylation of p150(GLUED)1A was also involved in Golgi reorientation in polarized cells. The authors noted that the predominant isoform of DCTN1, p150(GLUED)1B, lacks 20 amino acids in the basic microtubule-binding region, including the serine phosphorylated by SLK.
Collin et al. (1998) found that the DCTN1 gene spans approximately 19.4 kb of genomic DNA and consists of at least 32 exons ranging in size from 15 to 499 bp.
Pushkin et al. (2001) showed by Southern blot and BAC analyses that the DCTN1 and SLC4A5 (606757) proteins are encoded by a single locus. The DCTN1-SLC4A5 locus spans approximately 230 kb and contains 66 exons. Approximately 200 kb encode SLC4A5. DCTN1 is encoded by exons 1 through alternative exon 32. The same locus therefore uniquely encodes both a membrane protein (SLC4A5) and a cytoplasmic protein (DCTN1) with distinct functions.
Crystal Structure
Urnavicius et al. (2018) used electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein (600112) to dynactin. Whereas BICD2 (609797) is biased towards recruiting a single dynein, the adaptors BICDR1 (617002) and HOOK3 (607825) predominantly recruit 2 dyneins. Urnavicius et al. (2018) found that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. The 3.5-angstrom resolution cryoelectron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex revealed how dynactin can act as a scaffold to coordinate 2 dyneins side by side. Urnavicius et al. (2018) concluded that their work provided a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine.
By fluorescence in situ hybridization, Holzbaur and Tokito (1996) mapped the DCTN1 gene to 2p13. They noted that the location of the gene corresponds to that of a form of recessive limb-girdle muscular dystrophy (see LGMD2B; 253601). Also, this region of human chromosome 2 shows syntenic homology with a region of mouse chromosome 6 containing the mnd2 mouse mutation, which exhibits symptoms resembling human motor neuron disease.
Korthaus et al. (1997) presented evidence that the DCTN1 gene maps to chromosome 2 between TGFA and D2S1394.
Vilarino-Guell et al. (2009) sequenced the DCTN1 gene in 286 individuals with Parkinson disease (PD; 168600), frontotemporal lobar degeneration (FTLD; 600274), or amyotrophic lateral sclerosis (ALS; 105400). None of the 36 variants identified segregated conclusively within families, suggesting that DCTN1 mutations are rare and do not play a common role in these diseases. Further analysis of 440 patients with PD, 374 with FTLD, and 372 with ALS who lacked a family history also failed to find an association between DCTN1 variants and disease. In fact, the previously reported pathogenic mutation T1249I (601143.0002), which was identified in 3 of 435 controls, did not segregate in a large pedigree with Parkinson disease, thus weakening the evidence for the pathogenicity of this variant.
Autosomal Dominant Distal Hereditary Motor Neuronopathy 14
Puls et al. (2003) identified a gly59-to-ser mutation (601143.0001) in the DCTN1 gene in a family with slowly progressive autosomal dominant distal hereditary motor neuronopathy with vocal paresis (HMND14; 607641).
Susceptibility to Amyotrophic Lateral Sclerosis
Among 250 patients with a putative diagnosis of amyotrophic lateral sclerosis (ALS; 105400), Munch et al. (2004) identified 3 mutations in the DCTN1 gene (601143.0002-601143.0004) in 3 families. The authors distinguished the phenotype in their patients from that reported by Puls et al. (2003) by the presence of upper motor neuron signs, although specific clinical details were lacking. Munch et al. (2004) suggested that mutations in the DCTN1 gene may be a susceptibility factor for ALS.
Perry Syndrome
In affected members of 8 families with Perry syndrome (168605), Farrer et al. (2009) identified 5 different heterozygous mutations in the DCTN1 gene (see, e.g., 601143.0006-601143.0007). In vitro functional expression studies indicated that the mutations resulted in decreased microtubule binding and intracytoplasmic inclusions.
In 4 affected members of a large 3-generation French family with Perry syndrome, Caroppo et al. (2014) identified a heterozygous missense mutation in the DCTN1 gene (G71E; 601143.0008).
In a North American family with a slowly progressive, autosomal dominant form of lower motor neuron with vocal cord paresis but without sensory symptoms (HMND14; 607641), Puls et al. (2003) found a single-basepair change in the DCTN1 gene (c.957C-T) resulting in an amino acid substitution of serine for glycine at position 59 in affected family members. The G59S substitution occurred in the highly conserved CAP-Gly motif of the p150(Glued) subunit of dynactin, a domain that binds directly to microtubules. The transport protein dynactin is required for dynein-mediated retrograde transport of vesicles and organelles along microtubules. Overexpression of dynamitin (607376), the p50 subunit of the dynactin complex, disrupts the complex and produces a late-onset, progressive motor neuron disease in transgenic mice (LaMonte et al., 2002).
Variant Function
Using in vitro studies, Levy et al. (2006) demonstrated that the mutant G59S mutation disrupted the binding of DCTN1 to microtubules and to EB1 (603108). Studies of fibroblasts and lymphoblasts derived from patients with the mutation suggested that the mutant protein is expressed and incorporated into the dynactin complex. Under stress conditions, the mutant cells showed impaired recovery of Golgi complex morphology compared to controls, consistent with a subtle defect. The G59S mutation disrupted the folding of the CAP-Gly domain, resulting in aggregation of the mutant protein, which promoted cell death in a motor cell line. Overexpression of the chaperone Hsp70 (140550) inhibited aggregate formation and prevented cell death. These data suggested that the G59S mutation causes both a subtle loss of function and a gain of toxic function.
Based on crystal structure, gly59 is embedded in a beta-sheet. In budding yeast, Moore et al. (2009) generated a G59S-analogous mutation that resulted in complete loss of the CAP-Gly domain. Functional expression studies showed that the CAP-Gly domain has a critical role in the initiation and persistence of dynein-dependent movement of the mitotic spindle and nucleus, but was otherwise dispensable for dynein-based movement. The function also appeared to be context-dependent, such as during mitosis, indicating that CAP-Gly activity may only be necessary when dynein needs to overcome high force thresholds to produce movement. The CAP-Gly domain was not the primary link between dynactin and microtubules, although it was involved in the interaction.
In a woman with a disorder similar to amyotrophic lateral sclerosis (105400), Munch et al. (2004) identified a heterozygous 4546C-T transition in exon 13 of the DCTN1 gene, resulting in a thr1249-to-ile (T1249I) substitution. She had disease onset at age 56 years, with gait disturbance and distal lower limb muscle weakness and atrophy. The symptoms were slowly progressive over 4 years. There was no involvement of the upper limbs or bulbar region. There was no family history. The mutation was not identified in 150 control subjects. See also 607641.
Vilarino-Guell et al. (2009) identified the T1249I variant in 3 of 435 controls, 5 of 440 patients with Parkinson disease (168600), 1 of 374 with frontotemporal lobar degeneration (600274), and 5 of 372 patients with ALS. Lack of segregation of the variant in a large pedigree with Parkinson disease weakened the evidence for the pathogenicity of this variant.
In a woman with probable ALS (105400), Munch et al. (2004) identified a heterozygous 2512T-C transition in exon 15 of the DCTN1 gene, resulting in a met571-to-thr (M571T) substitution. She had onset of upper limb involvement at age 48 years and developed bulbar symptoms within 8 years. Her sister was similarly affected, although DNA was not available. The mutation was not identified in 150 control subjects.
In 2 brothers with probable ALS (105400), Munch et al. (2004) identified a heterozygous 3153C-T transition in exon 20 of the DCTN1 gene, resulting in an arg785-to-trp (R785W) substitution. The proband had upper limb onset at age 55 years, whereas his brother had bulbar onset at age 64 years. The asymptomatic mother and sister carried the same mutation, suggesting incomplete penetrance. The mutation was not identified in 150 control subjects.
In a patient with amyotrophic lateral sclerosis (105400), Munch et al. (2005) identified a heterozygous 4102G-A transition in the DCTN1 gene, resulting in an arg1101-to-lys (R1101K) substitution. The patient's brother, who also carried the R1101K mutation, had frontotemporal dementia without motor involvement. Family history revealed that 2 additional family members reportedly had motor neuron disease and frontotemporal dementia, respectively, but their DNA was not available for testing. The mutation was not identified in 500 control individuals. Despite the molecular findings, Munch et al. (2005) suggested that the R1101K variant may not be the primary gene defect in this family.
In affected members of 2 unrelated families with Perry syndrome (168605), Farrer et al. (2009) identified a heterozygous 211G-A transition in exon 2 of the DCTN1 gene, resulting in a gly71-to-arg (G71R) substitution at a highly conserved residue within the GKNDG binding motif of the CAP-Gly domain. The families were of Canadian and Turkish ancestry, respectively, and haplotype analysis excluded a founder effect. In vitro functional expression studies showed that the mutation decreased microtubule binding and resulted in intracytoplasmic inclusions. Farrer et al. (2009) also identified a different mutation in the same codon (G71E; 601143.0008) in patients with this disorder.
Newsway et al. (2010) identified a heterozygous G71R mutation in the DCTN1 gene in a man who developed symptoms in his mid-forties. In addition to parkinsonism, psychiatric disturbances, and weight loss, he showed signs of frontotemporal dementia as well as slowing of vertical downgaze and midbrain atrophy, reminiscent of progressive supranuclear palsy.
In affected members of a Japanese family with Perry syndrome (168605), Farrer et al. (2009) identified a heterozygous 221A-C transversion in exon 2 of the DCTN1 gene, resulting in a gln74-to-pro (Q74P) substitution at a highly conserved residue adjacent to the GKNDG binding motif of the CAP-Gly domain. In vitro functional expression studies showed that the mutation decreased microtubule binding and resulted in intracytoplasmic inclusions.
In 4 affected members of a 3-generation French family with various manifestations of a neurodegenerative disorder consistent with Perry syndrome (168605), Caroppo et al. (2014) identified a heterozygous c.212G-A transition in exon 2 of the DCTN1 gene, resulting in a gly71-to-glu (G71E) substitution at a highly conserved residue in the GKNDG domain. The mutation segregated with the disorder in the family and was not present in the Exome Variant Server database. In addition to the cardinal features of Perry syndrome, some patients showed frontotemporal dementia and features reminiscent of progressive supranuclear palsy. Functional studies of the variant were not performed.
This mutation had previously been reported by Farrer et al. (2009) in affected members of an unrelated French family with Perry syndrome. Farrer et al. (2009) also identified a different mutation in the same codon (G71R; 601143.0006) in patients with this disorder.
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