DVL1

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Dishevelled, dsh homolog 1 (Drosophila)
Protein DVL1 PDB 1fsh.png
PDB rendering based on 1fsh.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols DVL1 ; DVL; DVL1L1
External IDs OMIM601365 MGI94941 HomoloGene20926 ChEMBL: 6027 GeneCards: DVL1 Gene
Orthologs
Species Human Mouse
Entrez 1855 13542
Ensembl ENSG00000107404 ENSMUSG00000029071
UniProt O14640 P51141
RefSeq (mRNA) NM_004421 NM_010091
RefSeq (protein) NP_004412 NP_034221
Location (UCSC) Chr 1:
1.27 – 1.28 Mb
Chr 4:
155.85 – 155.86 Mb
PubMed search [1] [2]

Segment polarity protein dishevelled homolog DVL-1 is a protein that in humans is encoded by the DVL1 gene.[1][2]

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.[2]

Interactions[edit]

DVL1 has been shown to interact with DVL3,[3] EPS8,[4] AXIN1[5][6] and Mothers against decapentaplegic homolog 3.[7]

See also[edit]

References[edit]

  1. ^ Pizzuti A, Amati F, Calabrese G, Mari A, Colosimo A, Silani V, Giardino L, Ratti A, Penso D, Calza 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. 
  2. ^ a b "Entrez Gene: DVL1 dishevelled, dsh homolog 1 (Drosophila)". 
  3. ^ 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. (UNITED STATES) 19 (6): 4414–22. ISSN 0270-7306. PMC 104400. PMID 10330181. 
  4. ^ Inobe, M; Katsube K i; Miyagoe Y; Nabeshima Y i; Takeda S (Dec 1999). "Identification of EPS8 as a Dvl1-associated molecule". Biochem. Biophys. Res. Commun. (UNITED STATES) 266 (1): 216–21. doi:10.1006/bbrc.1999.1782. ISSN 0006-291X. PMID 10581192. 
  5. ^ Li, L; Yuan H; Weaver C D; Mao J; Farr G H; Sussman D J; 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. (ENGLAND) 18 (15): 4233–40. doi:10.1093/emboj/18.15.4233. ISSN 0261-4189. PMC 1171499. PMID 10428961. 
  6. ^ Kim, Min Jung; Chia Ian V; Costantini Frank (Nov 2008). "SUMOylation target sites at the C terminus protect Axin from ubiquitination and confer protein stability". FASEB J. (United States) 22 (11): 3785–94. doi:10.1096/fj.08-113910. PMC 2574027. PMID 18632848. 
  7. ^ Warner, Dennis R; Pisano M Michele; Roberts Emily A; Greene Robert M (Mar 2003). "Identification of three novel Smad binding proteins involved in cell polarity". FEBS Lett. (Netherlands) 539 (1–3): 167–73. doi:10.1016/S0014-5793(03)00155-8. ISSN 0014-5793. PMID 12650946. 

Further reading[edit]

External links[edit]