Alternative titles; symbols
HGNC Approved Gene Symbol: DVL1
Cytogenetic location: 1p36.33 Genomic coordinates (GRCh38): 1:1,335,278-1,349,418 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 1p36.33 | Robinow syndrome, autosomal dominant 2 | 616331 | Autosomal dominant | 3 |
The DVL1 gene encodes dishevelled-1, a member of a family of intracellular scaffolding proteins that act downstream of transmembrane WNT (164820) receptors. The Drosophila dishevelled gene (dsh) encodes a cytoplasmic phosphoprotein (Klingensmith et al., 1994) that regulates cell proliferation, acting as a transducer molecule for developmental processes, including segmentation and neuroblast specification. Pizzuti et al. (1996) noted that dsh is required for the function of the wingless gene product wg, a segment polarity gene homologous to the mammalian protooncogene WNT1.
Pizzuti et al. (1996) used oligonucleotides corresponding to the mouse dishevelled homolog (Dvl1) to isolate cDNA clones from a human fetal brain cDNA library and human adult caudate cDNA library. One human cDNA clone, designated DVL1 by them, encodes a 670-amino acid polypeptide that had 92% overall identity to the mouse Dvl1 protein (99% homology in the N-terminal half and 84% identity in the C-terminal half). By Northern blot analysis of poly(A) mRNA Pizzuti et al. (1996) observed a transcription product of approximately 2.9 kb with maximal expression in adult skeletal muscle and pancreas and abundant expression in heart muscle relative to a control transcript. Detectable levels were also found in adult brain, placenta, lung, liver, and kidney. The same expression patterns were found in fetal tissues. DVL1 expression was detected in the human neural tube (particularly in the dorsal portions) by in situ hybridization. DVL1 shares approximately 64% amino acid identity with DVL3 (601368). Pizzuti et al. (1996) concluded that the high level of homology in the N-terminal regions of these proteins indicates that the N-terminal regions encode essential domains for the whole class of dishevelled proteins, while the sequence divergence in the C-terminal half suggests that these regions contain domains which are responsible for specific single-molecule (i.e., DVL1 or DVL3) activity. They noted that 1 domain of DVL1 shows homology to the Drosophila discs large tumor suppressor gene dgl1 (601014).
Semenov and Snyder (1997) cloned and characterized 3 human homologs of dishevelled, thereby showing that these genes form a multigene family in humans. The cDNA sequence of DVL1 reported by Semenov and Snyder (1997) differs from that previously reported by Pizzuti et al. (1996). They also demonstrated that one of the human dishevelled homologs, DVL2 (602151), is a phosphoprotein, raising the possibility that the mechanisms of dishevelled function in Wnt signaling are likely to be conserved among metazoans.
Wallingford et al. (2000) used time-lapse confocal microscopy to demonstrate that the failure of cells lacking Xenopus dishevelled function to undergo convergent extension results from defects in cell polarity. Furthermore, Xenopus dishevelled mutations that inhibit convergent extension correspond to mutations in Drosophila dishevelled that selectively perturb planar cell polarity. Wallingford et al. (2000) concluded that polarized cell behavior is essential for convergent extension and is controlled by vertebrate dishevelled. Thus, a vertebrate equivalent of the Drosophila planar cell polarity signaling cascade may be required for normal gastrulation.
Luo et al. (2002) found that Dvl1 interacted with Musk (601296) in a mouse muscle cell line and in HEK293 cells transfected with mouse constructs. They determined that Dvl1 was expressed at a high level during development of embryonic mouse skeletal muscle, in a pattern that was similar to that of Musk, but expression decreased as development progressed. They further demonstrated that the Musk-Dvl1 interaction regulated acetylcholine receptor (see 100690) clustering stimulated by agrin (103320), and a mutant form of Dvl that did not interact with Musk inhibited the ability of agrin to induce receptor clustering.
From results of coimmunoprecipitation experiments, confocal microscopy analysis, and study of deletion mutants, Park and Moon (2002) concluded that the Dsh protein interacts with stbm, the zebrafish and Xenopus homolog of VANGL2 (600533).
Rosso et al. (2005) examined expression of endogenous Dvl1 in mouse hippocampal neurons and found Dvl1 localized in dendrites and axons, where it was associated with microtubules, and accumulated in actin-rich regions. Overexpression of Dvl1 increased dendritic branching in cultured hippocampal neurons, similar to the effect of Wnt7b (601967) overexpression, and branching was blocked by Sfrp1 (604156), a secreted Wnt antagonist. Conversely, hippocampal neurons from mice lacking Dvl1 showed reduced dendritic arborization. Analysis of downstream events showed that Wnt7b and Dvl1 regulate dendritic development through a noncanonical Wnt pathway by activating Rac (see 602048) and JNK (see 601158).
Dollar et al. (2005) demonstrated that a vertebrate homolog of Lgl (600966) associates with dishevelled, an essential mediator of Wnt signaling, and that dishevelled regulates the localization of Lgl in Xenopus ectoderm and Drosophila follicular epithelium. Dollar et al. (2005) showed that both Lgl and Dsh are required for normal apical-basal polarity of Xenopus ectodermal cells. In addition, Dollar et al. (2005) showed that the Wnt receptor frizzled-8 (606146), but not frizzled-7 (603410), causes Lgl to dissociate from the cortex with the concomitant loss of its activity in vivo. Dollar et al. (2005) concluded that their findings suggest a molecular basis for the regulation of cell polarity by frizzled and dishevelled.
Park et al. (2006) identified Dsh and Frodo (DACT1; 607861) as upstream regulators of the p120-catenin (CTNND1; 601045)/Kaiso (300329) signaling pathway in Xenopus.
Using live imaging of vertebrate cells, Bilic et al. (2007) demonstrated that the scaffold protein dishevelled (DVL) is required for LRP6 (603507) phosphorylation and aggregation following WNT treatment. Bilic et al. (2007) proposed that WNTs induce coclustering of receptors and DVL in LRP6 signalosomes, which in turn triggers LRP6 phosphorylation to promote Axin (603816) recruitment and beta-catenin (see 116806) stabilization.
Zhang et al. (2007) found that downregulation of Dvl abrogated axon differentiation in cultured embryonic rat hippocampal neurons, whereas overexpression of Dvl resulted in multiple axon formation. A complex of PAR3 (PARD3; 606745), PAR6 (PARD6A; 607484), and an atypical protein kinase C (aPKC), such as PKC-zeta (PRKCZ; 176982), is required for axon-dendrite differentiation, and Zhang et al. (2007) found that Dvl associated with Pkc-zeta in rat brain and transfected human embryonic kidney cells. The interaction of Dvl with Pkc-zeta resulted in stabilization and activation of Pkc-zeta. Expression of dominant-negative Pkc-zeta attenuated multiple axon formation due to Dvl overexpression in neurons, and overexpression of Pkc-zeta prevented axon loss due to Dvl downregulation. Wnt5a (164975), a noncanonical Wnt, activated Pkc-zeta and promoted axon differentiation, and downregulation of Dvl or inhibition of Pkc-zeta attenuated the Wnt5a effect on axon differentiation. Zhang et al. (2007) concluded that WNT5A and DVL promote axon differentiation mediated by the PAR3-PAR6-aPKC complex.
Mutations in the LRRK2 gene (609007) are the most common known cause of Parkinson disease (see PARK8; 607060). Sancho et al. (2009) reported interaction of LRRK2 with the dishevelled family of phosphoproteins DVL1, DVL2 (602151), and DVL3 (601368). The LRRK2 Roc-COR domain and the DVL1 DEP domain were necessary and sufficient for LRRK2-DVL1 interaction. Coexpression of DVL1 increased LRRK2 steady-state protein levels, an effect that was dependent on the DEP domain. LRRK2-DVL1-3 interactions were disrupted by the familial LRRK2 Y1699C mutation (609007.0002), whereas pathogenic mutations at residues arg1441 (see, e.g., 609007.0001) and arg1728 strengthened LRRK2-DVL1 interactions. Coexpression of DVL1 with LRRK2 in mammalian cells resulted in the redistribution of LRRK2 to typical cytoplasmic DVL1 aggregates in HEK293 and SH-SY5Y cells and colocalization in neurites and growth cones of differentiated dopaminergic SH-SY5Y cells. Since the DVL1 DEP domain is known to be involved in the regulation of small GTPases, Sancho et al. (2009) proposed that DVLs may influence LRRK2 GTPase activity, and that Roc-COR domain mutations modulating LRRK2-DVL interactions indirectly influence kinase activity.
Using nuclear magnetic resonance and fluorescence spectroscopy, Lee et al. (2010) confirmed direct interaction between the isolated C-terminal PDZ-binding domain of human TMEM88 (617813) and recombinant mouse Dvl1. Overexpression of TMEM88 in HEK293 cells attenuated WNT1-induced expression of a reporter gene in a dose-dependent manner and required the C-terminal PDZ-binding VWV motif of TMEM88. Conversely, knockdown of TMEM88 via RNA interference elevated Wnt signaling. In Xenopus larvae animal cap explants, human TMEM88 localized to cell membranes and inhibited Wnt signaling induced by Xenopus Dsh but not by beta-catenin. When coinjected, TMEM88 recruited fluorescence-tagged Dsh to cell membranes. Expression of human TMEM88 also inhibited secondary axis formation induced in Xenopus larvae by overexpressed Dsh. Since membrane-bound frizzled receptor (FZ; see 603408) promotes Wnt signaling by binding to the PDZ domain of DVL, Lee et al. (2010) hypothesized that TMEM88 counters Wnt signaling by inhibiting FZ-DVL interaction.
Shafer et al. (2011) found that both Dvl1 and Vangl2 were required for Wnt5a-stimulated outgrowth and anterior-posterior guidance of embryonic mouse and rat commissural axons. Dvl1 inhibited PCP signaling by increasing hyperphosphorylation of Frizzled-3 (FZD3; 606143), preventing its internalization. Vangl2 antagonized Fzd3 phosphorylation and promoted its internalization. In rat commissural axon growth cones, Vangl2 predominantly localized on the plasma membrane and was highly enriched on tips of filopodia, as well as in patches of membrane where new filopodia emerged. Shafer et al. (2011) proposed that the antagonistic functions of VANGL2 and DVL3 on FZD3 hyperphosphorylation and endocytosis sharpen PCP signaling at the tips of filopodia to sense directional Wnt signaling to cause turning of growth cones.
By analysis of a panel of rodent-human somatic cell hybrids by PCR with primers for the DVL1 3-prime untranslated region, Pizzuti et al. (1996) mapped the DVL1 gene to human chromosome 1. They used fluorescence in situ hybridization with cloned cDNAs to map the DVL1 gene to chromosome 1p36. Pizzuti et al. (1996) noted that the region of DVL1 that shows homology to the Drosophila tumor suppressor gene dgl1, as well as its possible role as a neural differentiation factor, would make it a candidate gene for neuroblastomatous transformation (see also 256700, the 1p36-linked neuroblastoma locus). The Schwartz-Jampel syndrome (255800) has been mapped to chromosome 1p36-p34 and Pizzuti et al. (1996) suggested that the phenotype of this disease is consistent with defects which might be expected from aberrant expression of a DVL gene during development. They noted also that Charcot-Marie-Tooth disease type 2A (118210) has been mapped to 1p36-1p35 and that the main pathologic feature of this disorder is a motor neuron axonal degeneration. See also the dishevelled-like locus that maps to the DiGeorge critical region on chromosome 22q11 (601225).
Bedell et al. (1996) characterized the region of deletion in a patient with the 1p36 deletion syndrome (607872) whose karyotype was 46,XY, del(1)(p36.3). They identified the dishevelled gene within the deleted region. The authors speculated that this gene may play a role in the pathogenesis of the observed syndrome through haploinsufficiency or through genomic imprinting, which had been reported previously for this region of chromosome 1 by Caron et al. (1995).
In 8 patients, including a pair of monozygotic twins, with autosomal dominant Robinow syndrome-2 (DRS2; 616331), White et al. (2015) identified 6 different de novo heterozygous truncating mutations in the DVL1 gene (see, e.g., 601365.0001-601365.0004). Mutations in the first 3 patients were found by whole-exome sequencing; subsequent patients were identified from a cohort of 62 additional individuals with a similar phenotype who underwent targeted sequencing of the DVL1 gene. Functional studies of the variants were not performed, but studies of 2 patients' cells showed that the truncated proteins were expressed.
In 3 unrelated patients with DRS2, Bunn et al. (2015) identified 3 different heterozygous mutations in the DVL1 gene (601365.0004-610365.0006), all of which resulted in premature termination of the protein and addition of an abnormal highly basic C-terminal sequence. Analysis of cells from 1 of the patients showed that the mutation (c.1519del; 601365.0004) was translated into a stable protein and not degraded by nonsense-mediated mRNA decay. In vitro cellular expression studies showed that cotransfection of the mutation with wildtype DVL1 resulted in increased canonical WNT activity.
Human evolution is characterized by a dramatic increase in brain size and complexity. To probe its genetic basis, Dorus et al. (2004) examined the evolution of genes involved in diverse aspects of nervous system biology. These genes, including DVL1, displayed significantly higher rates of protein evolution in primates than in rodents. This trend was most pronounced for the subset of genes implicated in nervous system development. Moreover, within primates, the acceleration of protein evolution was most prominent in the lineage leading from ancestral primates to humans. Dorus et al. (2004) concluded that the phenotypic evolution of the human nervous system has a salient molecular correlate, i.e., accelerated evolution of the underlying genes, particularly those linked to nervous system development.
Lijam et al. (1997) created Dvl1-null mice by gene targeting. Dvl1-deficient mice are viable, fertile, and structurally normal. However, these mice exhibited reduced social interaction, manifested as decreased whisker trimming, deficits in nest building, less huddling contact during sleep, and subordinate responses in a social dominance test. Sensorimotor gating was abnormal, as measured by deficits in prepulse inhibition of acoustic and tactile startle. Since reduced social interaction and abnormal sensorimotor gating are features of several human neuropsychiatric disorders, including schizophrenia, Lijam et al. (1997) suggested that Dvl1-deficient mice may provide a model for aspects of these disorders. Lijam et al. (1997) concluded that these results were consistent with an interpretation that common genetic mechanisms underlie abnormal social behavior and implicated Dvl1 in processes underlying complex behaviors.
In 2 unrelated patients (BAB4878 and 016462) with autosomal dominant Robinow syndrome-2 (DRS2; 616331), White et al. (2015) identified a de novo heterozygous 13-bp deletion (c.1505_1517del, NM_004421.2) in exon 14 of the DVL1 gene, resulting in a frameshift and premature termination (His502ProfsTer143). The mutation in the first patient was found by whole-exome sequencing and confirmed by Sanger sequencing. The second patient was identified from a cohort of 62 additional individuals with a similar phenotype who underwent targeted sequencing of the DVL1 gene. The mutation was not found in publicly available databases or in an in-house database. Functional studies of the variant were not performed.
In a patient (BAB4073) with autosomal dominant Robinow syndrome-2 (DRS2; 616331), White et al. (2015) identified a de novo heterozygous deletion (TT)/insertion (C) mutation (c.1570_1571delins, NM_004421.2) in exon 14 of the DVL1 gene, resulting in a frameshift and premature termination (Phe524ProfsTer125). The mutation was found by whole-exome sequencing and confirmed by Sanger sequencing. RT-PCR analysis of patient cells showed that the mutation escaped nonsense-mediated mRNA decay and that the truncated protein was expressed. The mutation was not found in publicly available databases or in an in-house database. Functional studies of the variant were not performed.
In a pair of monozygotic twins (016516 and 016517) with autosomal dominant Robinow syndrome-2 (DRS2; 616331) originally reported by Saraiva et al. (1999), White et al. (2015) identified a de novo heterozygous 1-bp deletion of a C nucleotide (c.1508del, NM_004421.2) in exon 14 of the DVL1 gene, resulting in a frameshift and premature termination (Pro503ArgfsTer146). The mutation was not found in publicly available databases or in an in-house database. Functional studies of the variant were not performed.
In a 6-year-old boy (patient BAB5264) with autosomal dominant Robinow syndrome-2 (DRS2; 616331), White et al. (2015) identified heterozygosity for a 1-bp deletion of a T nucleotide at nucleotide 1519 in exon 14 of the DVL1 gene (c.1519del, NM_004421.2). The deletion, identified by whole-exome sequencing, resulted in a frameshift and premature termination of the protein (Trp507GlyfsTer142). Bunn et al. (2015) detected this mutation in a patient originally reported by Bunn et al. (2014) (patient 1 in both studies) and showed it to occur de novo in their patient. Bunn et al. (2015) found the mutation by whole-exome sequencing and validated it by Sanger sequencing; it was not found in the Exome Variant Server (ESP6500) database or in 400 in-house control exomes. Analysis of cells from the patient showed that the mutation was translated into a stable protein and not degraded by nonsense-mediated mRNA decay. In vitro cellular expression studies showed that cotransfection of the mutation with wildtype DVL1 resulted in increased canonical WNT activity.
In a patient with autosomal dominant Robinow syndrome-2 (DRS2; 616331) originally reported by Bunn et al. (2014) (patient 2 in both reports), Bunn et al. (2015) identified a de novo heterozygous 1-bp deletion (c.1562del, NM_004421.2) in exon 14 of the DVL1 gene, resulting in a frameshift and premature termination (Pro521HisfsTer128).
In a patient (patient 3) with autosomal dominant Robinow syndrome-2 (DRS2; 616331) originally reported by Eijkenboom et al. (2012), Bunn et al. (2015) identified a de novo heterozygous del/ins mutation (c.1576_1583delinsG, NM_004421.2) in exon 14 of the DVL1 gene, resulting in a frameshift and premature termination (Pro526AlafsTer121).
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