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DVL1 Contents Function Interactions See also References Further reading External links Navigation menuPDBeRCSB1FSH1MC72KAW3PZ8DVL19494120926DVL1Rac GTPase bindingbeta-catenin bindingfrizzled bindingprotein bindingidentical protein bindingenzyme bindingprotein kinase bindingcytoplasmcytosolWnt signalosomelateral plasma membranemembranemicrotubule cytoskeletongrowth coneplasma membranesynapseaxonneuronal cell bodydendriteneuron projectionmicrotubuleclathrin-coated vesiclepresynapsedendritic spinepostsynaptic densitycytoplasmic vesicleSchaffer collateral - CA1 synapseglutamatergic synapseregulation of protein phosphorylationnegative regulation of protein phosphorylationregulation of neurotransmitter levelspositive regulation of protein phosphorylationintracellular signal transductionaxonogenesisnegative regulation of protein kinase activitydendrite morphogenesissynapse organizationprotein stabilizationregulation of cellular protein localizationWnt signaling pathwaytranscription from RNA polymerase II promoternegative regulation of protein bindingreceptor clusteringplanar cell polarity pathway involved in neural tube closureaxon guidancepositive regulation of transcription, DNA-templatedpositive regulation of Wnt signaling pathwaymulticellular organism developmentWnt signaling pathway, planar cell polarity pathwayprotein localization to microtubuleneuromuscular junction developmentcochlea morphogenesisneural tube developmentcytoplasmic microtubule organizationpositive regulation of neuron projection developmentaxon extensionprotein localization to nucleuscanonical Wnt signaling pathwaysocial organism behaviorskeletal muscle acetylcholine-gated channel clusteringcollateral sproutingconvergent extension involved in neural plate elongationnegative regulation of canonical Wnt signaling pathwayneurotransmitter secretionpositive regulation of proteasomal ubiquitin-dependent protein catabolic processconvergent extension involved in organogenesisprepulse inhibitionpositive regulation of canonical Wnt signaling pathwaybeta-catenin destruction complex disassemblydendritic spine morphogenesispositive regulation of excitatory postsynaptic potentialpresynapse assemblypositive regulation of protein localization to presynapsenon-canonical Wnt signaling pathwaypostsynapse organizationpositive regulation of neuron projection arborizationregulation of synaptic vesicle exocytosisAmigoQuickGO185513542ENSG00000107404ENSMUSG00000029071O14640P51141NM_004421NM_181870NM_182779NM_001330311NM_010091NM_001302342NM_001356381NP_001317240NP_004412NP_001289271NP_034221NP_001343310Chr 1: 1.34 – 1.35 MbChr 4: 155.85 – 155.86 MbGRCh38: Ensembl release 89: ENSG00000107404GRCm38: Ensembl release 89: ENSMUSG00000029071"Human PubMed Reference:""Mouse PubMed Reference:"10.1093/hmg/5.7.9538817329"Entrez Gene: DVL1 dishevelled, dsh homolog 1 (Drosophila)""Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1"10.1093/emboj/18.15.4233117149910428961"SUMOylation target sites at the C terminus protect Axin from ubiquitination and confer protein stability"10.1096/fj.08-113910257402718632848"DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability"10.1128/mcb.19.6.44141044001033018110.1006/bbrc.1999.17821058119210.1016/s0014-5793(03)00155-81265094610.1006/dbio.2002.08691249019410.1101/gad.8.1.1188288125"Human homologue sequences to the Drosophila dishevelled segment-polarity gene are deleted in the DiGeorge syndrome"1914677864473410.1007/BF02723007885634510.1006/geno.1997.4713919285110.1006/bbrc.1997.75009344861"Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin"10.1093/emboj/17.5.137111704859482734"DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability"10.1128/mcb.19.6.441410440010330181"Domains of axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization"10.1083/jcb.145.4.741213317910330403"Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1"10.1093/emboj/18.15.423311714991042896110.1074/jbc.275.4.23991064469110.1074/jbc.M90910719910806215"Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding protein"10.1128/MCB.21.1.330-342.2001888061111320710.1074/jbc.M10514820011487578"beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins"10.1073/pnas.211572798649541174207310.1016/S0092-8674(01)00614-61177946110.1038/sj/mp/400094111803455"Casein kinase I phosphorylates and destabilizes the beta-catenin degradation complex"10.1073/pnas.03246819912216411818547DVL1eexpanding ite

Genes on human chromosome 1Protein stubs

185513542ENSG00000107404ENSMUSG00000029071O14640P51141proteingenedishevelledphosphoproteincell proliferationneuroblastneuroblastomaSchwartz-Jampel syndromeCharcot-Marie-Tooth diseaseinteract

‹ The template Infobox gene is being considered for merging. ›

DVL1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1FSH, 1MC7, 2KAW, 3PZ8
Identifiers
Aliases	DVL1, DVL, DVL1L1, DVL1P1, DRS2, dishevelled segment polarity protein 1
External IDs	MGI: 94941 HomoloGene: 20926 GeneCards: DVL1
Gene location (Human) Chr. Chromosome 1 (human)[1] Band 1p36.33 Start 1,335,276 bp[1] End 1,349,418 bp[1]
Gene location (Mouse) Chr. Chromosome 4 (mouse)[2] Band 4 E2|4 87.61 cM Start 155,847,402 bp[2] End 155,859,303 bp[2]
Gene ontology Molecular function • Rac GTPase binding • beta-catenin binding • frizzled binding • protein binding • identical protein binding • enzyme binding • protein kinase binding Cellular component • cytoplasm • cytosol • Wnt signalosome • lateral plasma membrane • membrane • microtubule cytoskeleton • growth cone • plasma membrane • synapse • axon • neuronal cell body • dendrite • neuron projection • microtubule • clathrin-coated vesicle • presynapse • dendritic spine • postsynaptic density • cytoplasmic vesicle • Schaffer collateral - CA1 synapse • glutamatergic synapse Biological process • regulation of protein phosphorylation • negative regulation of protein phosphorylation • regulation of neurotransmitter levels • positive regulation of protein phosphorylation • intracellular signal transduction • axonogenesis • negative regulation of protein kinase activity • dendrite morphogenesis • synapse organization • protein stabilization • regulation of cellular protein localization • Wnt signaling pathway • transcription from RNA polymerase II promoter • negative regulation of protein binding • receptor clustering • planar cell polarity pathway involved in neural tube closure • axon guidance • positive regulation of transcription, DNA-templated • positive regulation of Wnt signaling pathway • multicellular organism development • Wnt signaling pathway, planar cell polarity pathway • protein localization to microtubule • neuromuscular junction development • cochlea morphogenesis • neural tube development • cytoplasmic microtubule organization • positive regulation of neuron projection development • axon extension • protein localization to nucleus • canonical Wnt signaling pathway • social organism behavior • skeletal muscle acetylcholine-gated channel clustering • collateral sprouting • convergent extension involved in neural plate elongation • negative regulation of canonical Wnt signaling pathway • neurotransmitter secretion • positive regulation of proteasomal ubiquitin-dependent protein catabolic process • convergent extension involved in organogenesis • prepulse inhibition • positive regulation of canonical Wnt signaling pathway • beta-catenin destruction complex disassembly • dendritic spine morphogenesis • positive regulation of excitatory postsynaptic potential • presynapse assembly • positive regulation of protein localization to presynapse • non-canonical Wnt signaling pathway • postsynapse organization • positive regulation of neuron projection arborization • regulation of synaptic vesicle exocytosis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	1855	13542
Ensembl	ENSG00000107404	ENSMUSG00000029071
UniProt	O14640	P51141
RefSeq (mRNA)	NM_004421 NM_181870 NM_182779 NM_001330311	NM_010091 NM_001302342 NM_001356381
RefSeq (protein)	NP_001317240 NP_004412	NP_001289271 NP_034221 NP_001343310
Location (UCSC)	Chr 1: 1.34 – 1.35 Mb	Chr 4: 155.85 – 155.86 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Segment polarity protein dishevelled homolog DVL-1 is a protein that in humans is encoded by the DVL1 gene.^[5][6]

Contents

• 
  1 Function
  


• 
  2 Interactions
  


• 
  3 See also
  


• 
  4 References
  


• 
  5 Further reading
  


• 
  6 External links
  

Function

DVL1, the human homolog of the Drosophila dishevelled gene (dsh) encodes a cytoplasmic phosphoprotein that regulates cell proliferation, acting as a transducer molecule for developmental processes, including segmentation and neuroblast specification. DVL1 is a candidate gene for processes involved in cell transformations involved in neuroblastoma. The Schwartz-Jampel syndrome and Charcot-Marie-Tooth disease type 2A have been mapped to the same region as DVL1. The phenotypes of these diseases may be consistent with defects which might be expected from aberrant expression of a DVL gene during development. Three transcript variants encoding three different isoforms have been found for this gene.^[6]

Interactions

DVL1 has been shown to interact with:

• 
  AXIN1,^[7][8]


• 
  DVL3,^[9]


• 
  EPS8,^[10] and


• 
  Mothers against decapentaplegic homolog 3.^[11]

See also

• Dishevelled

References

1. 
   ^ ^abc GRCh38: Ensembl release 89: ENSG00000107404 - Ensembl, May 2017
   


2. 
   ^ ^abc GRCm38: Ensembl release 89: ENSMUSG00000029071 - Ensembl, May 2017
   


3. 
   ^ "Human PubMed Reference:"..mw-parser-output cite.citationfont-style:inherit.mw-parser-output .citation qquotes:"""""""'""'".mw-parser-output .citation .cs1-lock-free abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .citation .cs1-lock-subscription abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registrationcolor:#555.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration spanborder-bottom:1px dotted;cursor:help.mw-parser-output .cs1-ws-icon abackground:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center.mw-parser-output code.cs1-codecolor:inherit;background:inherit;border:inherit;padding:inherit.mw-parser-output .cs1-hidden-errordisplay:none;font-size:100%.mw-parser-output .cs1-visible-errorfont-size:100%.mw-parser-output .cs1-maintdisplay:none;color:#33aa33;margin-left:0.3em.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-formatfont-size:95%.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-leftpadding-left:0.2em.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-rightpadding-right:0.2em
   


4. 
   ^ "Mouse PubMed Reference:".
   


5. 
   ^ Pizzuti A, Amati F, Calabrese G, Mari A, Colosimo A, Silani V, Giardino L, Ratti A, Penso D, Calzà L, Palka G, Scarlato G, Novelli G, Dallapiccola B (Jan 1997). "cDNA characterization and chromosomal mapping of two human homologues of the Drosophila dishevelled polarity gene". Hum Mol Genet. 5 (7): 953–8. doi:10.1093/hmg/5.7.953. PMID 8817329.
   


6. 
   ^ ^ab "Entrez Gene: DVL1 dishevelled, dsh homolog 1 (Drosophila)".
   


7. 
   ^ Li L, Yuan H, Weaver CD, Mao J, Farr GH, Sussman DJ, Jonkers J, Kimelman D, Wu D (Aug 1999). "Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1". EMBO J. 18 (15): 4233–40. doi:10.1093/emboj/18.15.4233. PMC 1171499. PMID 10428961.
   


8. 
   ^ Kim MJ, Chia IV, Costantini F (Nov 2008). "SUMOylation target sites at the C terminus protect Axin from ubiquitination and confer protein stability". FASEB J. 22 (11): 3785–94. doi:10.1096/fj.08-113910. PMC 2574027. PMID 18632848.
   


9. 
   ^ Kishida S, Yamamoto H, Hino S, Ikeda S, Kishida M, Kikuchi A (Jun 1999). "DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability". Mol. Cell. Biol. 19 (6): 4414–22. doi:10.1128/mcb.19.6.4414. PMC 104400. PMID 10330181.
   


10. 
    ^ Inobe M, Katsube Ki, Miyagoe Y, Nabeshima Yi, Takeda S (Dec 1999). "Identification of EPS8 as a Dvl1-associated molecule". Biochem. Biophys. Res. Commun. 266 (1): 216–21. doi:10.1006/bbrc.1999.1782. PMID 10581192.
    


11. 
    ^ Warner DR, Pisano MM, Roberts EA, Greene RM (Mar 2003). "Identification of three novel Smad binding proteins involved in cell polarity". FEBS Lett. 539 (1–3): 167–73. doi:10.1016/s0014-5793(03)00155-8. PMID 12650946.
    

Further reading

.mw-parser-output .refbeginfont-size:90%;margin-bottom:0.5em.mw-parser-output .refbegin-hanging-indents>ullist-style-type:none;margin-left:0.mw-parser-output .refbegin-hanging-indents>ul>li,.mw-parser-output .refbegin-hanging-indents>dl>ddmargin-left:0;padding-left:3.2em;text-indent:-3.2em;list-style:none.mw-parser-output .refbegin-100font-size:100%

• 
  Wharton KA (2003). "Runnin' with the Dvl: proteins that associate with Dsh/Dvl and their significance to Wnt signal transduction". Dev. Biol. 253 (1): 1–17. doi:10.1006/dbio.2002.0869. PMID 12490194.
  


• 
  Klingensmith J, Nusse R, Perrimon N (1994). "The Drosophila segment polarity gene dishevelled encodes a novel protein required for response to the wingless signal". Genes Dev. 8 (1): 118–30. doi:10.1101/gad.8.1.118. PMID 8288125.
  


• 
  Pizzuti A, Novelli G, Mari A, Ratti A, Colosimo A, Amati F, Penso D, Sangiuolo F, Calabrese G, Palka G, Silani V, Gennarelli M, Mingarelli R, Scarlato G, Scambler P, Dallapiccola B (1996). "Human homologue sequences to the Drosophila dishevelled segment-polarity gene are deleted in the DiGeorge syndrome". Am. J. Hum. Genet. 58 (4): 722–9. PMC 1914677. PMID 8644734.
  


• 
  Steitz SA, Tsang M, Sussman DJ (1997). "Wnt-mediated relocalization of dishevelled proteins". In Vitro Cell. Dev. Biol. Anim. 32 (7): 441–5. doi:10.1007/BF02723007. PMID 8856345.
  


• 
  Semënov MV, Snyder M (1997). "Human dishevelled genes constitute a DHR-containing multigene family". Genomics. 42 (2): 302–10. doi:10.1006/geno.1997.4713. PMID 9192851.
  


• 
  Bui TD, Beier DR, Jonssen M, Smith K, Dorrington SM, Kaklamanis L, Kearney L, Regan R, Sussman DJ, Harris AL (1997). "cDNA cloning of a human dishevelled DVL-3 gene, mapping to 3q27, and expression in human breast and colon carcinomas". Biochem. Biophys. Res. Commun. 239 (2): 510–6. doi:10.1006/bbrc.1997.7500. PMID 9344861.
  


• 
  Ikeda S, Kishida S, Yamamoto H, Murai H, Koyama S, Kikuchi A (1998). "Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin". EMBO J. 17 (5): 1371–84. doi:10.1093/emboj/17.5.1371. PMC 1170485. PMID 9482734.
  


• 
  Kishida S, Yamamoto H, Hino S, Ikeda S, Kishida M, Kikuchi A (1999). "DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability". Mol. Cell. Biol. 19 (6): 4414–22. doi:10.1128/mcb.19.6.4414. PMC 104400. PMID 10330181.
  


• 
  Fagotto F, Jho Eh, Zeng L, Kurth T, Joos T, Kaufmann C, Costantini F (1999). "Domains of axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization". J. Cell Biol. 145 (4): 741–56. doi:10.1083/jcb.145.4.741. PMC 2133179. PMID 10330403.
  


• 
  Li L, Yuan H, Weaver CD, Mao J, Farr GH, Sussman DJ, Jonkers J, Kimelman D, Wu D (1999). "Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1". EMBO J. 18 (15): 4233–40. doi:10.1093/emboj/18.15.4233. PMC 1171499. PMID 10428961.
  


• 
  Strovel ET, Wu D, Sussman DJ (2000). "Protein phosphatase 2Calpha dephosphorylates axin and activates LEF-1-dependent transcription". J. Biol. Chem. 275 (4): 2399–403. doi:10.1074/jbc.275.4.2399. PMID 10644691.
  


• 
  Song DH, Sussman DJ, Seldin DC (2000). "Endogenous protein kinase CK2 participates in Wnt signaling in mammary epithelial cells". J. Biol. Chem. 275 (31): 23790–7. doi:10.1074/jbc.M909107199. PMID 10806215.
  


• 
  Hino S, Kishida S, Michiue T, Fukui A, Sakamoto I, Takada S, Asashima M, Kikuchi A (2001). "Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding protein". Mol. Cell. Biol. 21 (1): 330–42. doi:10.1128/MCB.21.1.330-342.2001. PMC 88806. PMID 11113207.
  


• 
  Rubinfeld B, Tice DA, Polakis P (2001). "Axin-dependent phosphorylation of the adenomatous polyposis coli protein mediated by casein kinase 1epsilon". J. Biol. Chem. 276 (42): 39037–45. doi:10.1074/jbc.M105148200. PMID 11487578.
  


• 
  Chen W, Hu LA, Semenov MV, Yanagawa S, Kikuchi A, Lefkowitz RJ, Miller WE (2002). "beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 14889–94. doi:10.1073/pnas.211572798. PMC 64954. PMID 11742073.
  


• 
  Habas R, Kato Y, He X (2002). "Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1". Cell. 107 (7): 843–54. doi:10.1016/S0092-8674(01)00614-6. PMID 11779461.
  


• 
  Russ C, Lovestone S, Powell JF (2002). "Identification of genomic organisation, sequence variants and analysis of the role of the human dishevelled 1 gene in late onset Alzheimer's disease". Mol. Psychiatry. 7 (1): 104–9. doi:10.1038/sj/mp/4000941. PMID 11803455.
  


• 
  Gao ZH, Seeling JM, Hill V, Yochum A, Virshup DM (2002). "Casein kinase I phosphorylates and destabilizes the beta-catenin degradation complex". Proc. Natl. Acad. Sci. U.S.A. 99 (3): 1182–7. doi:10.1073/pnas.032468199. PMC 122164. PMID 11818547.
  

External links

• 
  DVL1 on the Atlas of Genetics and Oncology
  

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