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Doublecortin Edit Wikipedia article
PDB rendering based on 1mjd.
|Symbols||; DBCN; DC; LISX; SCLH; XLIS|
|RNA expression pattern|
Doublecortin (DCX) is a microtubule-associated protein expressed by neuronal precursor cells and immature neurons in embryonic and adult cortical structures. Neuronal precursor cells begin to express DCX while actively dividing, and their neuronal daughter cells continue to express DCX for 2–3 weeks as the cells mature into neurons. Downregulation of DCX begins after 2 weeks, and occurs at the same time that these cells begin to express, NeuN, a marker for mature neurons.
Due to the nearly exclusive expression of DCX in developing neurons, this protein has been used increasingly as a marker for neurogenesis. Indeed, the levels of DCX expression increase in response to exercise, which occurs in parallel with increased BrdU labelling, currently a "gold standard" in measuring neurogenesis.
Doublecortin was found to bind to the microtubule cytoskeleton. In vivo and in vitro assays show that Doublecortin stabilises microtubules and causes bundling. Doublecortin is a basic protein with an iso-electric point of 10, typical of microtubule-binding proteins.
solution structure of the N-terminal dcx domain of human doublecortin-like kinase
The detailed sequence analysis of Doublecortin and Doublecortin-like proteins allowed the identification of an tandem repeat of evolutionarily conserved Doublecortin (DC) domains. These domains are found in the N terminus of proteins and consists of tandemly repeated copies of an around 80 amino acids region. It has been suggested that the first DC domain of Doublecortin binds tubulin and enhances microtubule polymerisation.
Doublecortin has been shown to influence the structure of microtubules. Microtubule nucleated in vitro in the presence of Doublecortin have almost exclusively 13 protofilaments, whereas microtubule nucleated without Doublecortin are present in a range of different sizes.
Doublecortin is mutated in X-linked lissencephaly and the double cortex syndrome. X-linked lissencephaly produces a smooth brain due to lack of migration of immature neurons, without normal folding of the brain surface. Double cortex syndrome is characterized by abnormal migration of neural tissue during development which results in two bands of misplaced neurons within the subcortical white, generating two cortices, giving the name to the syndrome. Clinically, patients with X-linked lissencephaly are oftentimes male with a mutation in one of their X chromosomes. In the case of double cortex, the majority of patients are females with a mutation in one of the X-chromosomes, normally presenting with intractable seizures and mental retardation. The severity of the disease can be implied by a gene dosage effect, meaning that in the case of males, with only one X chromosome, there is no protein, however in the case of females with two X chromosome, the mutation in one X chromosome can somehow be compensated, however not enough functional protein is produced in the double cortex patients. The mutation was discovered by Joseph Gleeson and Christopher A. Walsh in Boston.
- EntrezGene 1641
- Oomen CA, Girardi CE, Cahyadi R, Verbeek EC, Krugers H, Joëls M, Lucassen PJ (2009). "Opposite effects of early maternal deprivation on neurogenesis in male versus female rats". PLoS ONE 4 (1): e3675. doi:10.1371/journal.pone.0003675. PMC 2629844. PMID 19180242.
- Brown JP, Couillard-Després S, Cooper-Kuhn CM, Winkler J, Aigner L, Kuhn HG (December 2003). "Transient expression of doublecortin during adult neurogenesis". J. Comp. Neurol. 467 (1): 1–10. doi:10.1002/cne.10874. PMID 14574675.
- Couillard-Despres S, Winner B, Schaubeck S, Aigner R, Vroemen M, Weidner N, Bogdahn U, Winkler J, Kuhn HG, Aigner L (January 2005). "Doublecortin expression levels in adult brain reflect neurogenesis". Eur. J. Neurosci. 21 (1): 1–14. doi:10.1111/j.1460-9568.2004.03813.x. PMID 15654838.
- Horesh D, Sapir T, Francis F, Wolf SG, Caspi M, Elbaum M, Chelly J, Reiner O (September 1999). "Doublecortin, a stabilizer of microtubules". Hum. Mol. Genet. 8 (9): 1599–610. doi:10.1093/hmg/8.9.1599. PMID 10441322.
- Sapir T, Horesh D, Caspi M, Atlas R, Burgess HA, Wolf SG, Francis F, Chelly J, Elbaum M, Pietrokovski S, Reiner O (March 2000). "Doublecortin mutations cluster in evolutionarily conserved functional domains". Hum. Mol. Genet. 9 (5): 703–12. doi:10.1093/hmg/9.5.703. PMID 10749977.
- Caspi M, Atlas R, Kantor A, Sapir T, Reiner O (September 2000). "Interaction between LIS1 and doublecortin, two lissencephaly gene products". Hum. Mol. Genet. 9 (15): 2205–13. doi:10.1093/oxfordjournals.hmg.a018911. PMID 11001923.
- Online 'Mendelian Inheritance in Man' (OMIM) Doublecortin -300121
- Gleeson JG, Allen KM, Fox JW, Lamperti ED, Berkovic S, Scheffer I, Cooper EC, Dobyns WB, Minnerath SR, Ross ME, Walsh CA (January 1998). "Doublecortin, a brain-specific gene mutated in human X-linked lissencephaly and double cortex syndrome, encodes a putative signaling protein". Cell 92 (1): 63–72. doi:10.1016/S0092-8674(00)80899-5. PMID 9489700.
- Lowenstein DH (2011). "Seizures and Epilepsy". In Loscalzo J, Longo DL, Fauci AS, Kasper DL, Hauser SL. Harrison's Principles of Internal Medicine (18th ed.). McGraw-Hill Professional. pp. 3251–3269. ISBN 0-07-174889-X.
- des Portes V, Pinard JM, Smadja D; et al. (1997). "Dominant X linked subcortical laminar heterotopia and lissencephaly syndrome (XSCLH/LIS): evidence for the occurrence of mutation in males and mapping of a potential locus in Xq22.". J. Med. Genet. 34 (3): 177–83. doi:10.1136/jmg.34.3.177. PMC 1050888. PMID 9132485.
- des Portes V, Pinard JM, Billuart P; et al. (1998). "A novel CNS gene required for neuronal migration and involved in X-linked subcortical laminar heterotopia and lissencephaly syndrome.". Cell 92 (1): 51–61. doi:10.1016/S0092-8674(00)80898-3. PMID 9489699.
- Gleeson JG, Allen KM, Fox JW; et al. (1998). "Doublecortin, a brain-specific gene mutated in human X-linked lissencephaly and double cortex syndrome, encodes a putative signaling protein.". Cell 92 (1): 63–72. doi:10.1016/S0092-8674(00)80899-5. PMID 9489700.
- des Portes V, Francis F, Pinard JM; et al. (1999). "doublecortin is the major gene causing X-linked subcortical laminar heterotopia (SCLH).". Hum. Mol. Genet. 7 (7): 1063–70. doi:10.1093/hmg/7.7.1063. PMID 9618162.
- Sossey-Alaoui K, Hartung AJ, Guerrini R; et al. (1998). "Human doublecortin (DCX) and the homologous gene in mouse encode a putative Ca2+-dependent signaling protein which is mutated in human X-linked neuronal migration defects.". Hum. Mol. Genet. 7 (8): 1327–32. doi:10.1093/hmg/7.8.1327. PMID 9668176.
- Pilz DT, Matsumoto N, Minnerath S; et al. (1999). "LIS1 and XLIS (DCX) mutations cause most classical lissencephaly, but different patterns of malformation.". Hum. Mol. Genet. 7 (13): 2029–37. doi:10.1093/hmg/7.13.2029. PMID 9817918.
- Gleeson JG, Minnerath SR, Fox JW; et al. (1999). "Characterization of mutations in the gene doublecortin in patients with double cortex syndrome.". Ann. Neurol. 45 (2): 146–53. doi:10.1002/1531-8249(199902)45:2<146::AID-ANA3>3.0.CO;2-N. PMID 9989615.
- Kato M, Kimura T, Lin C; et al. (1999). "A novel mutation of the doublecortin gene in Japanese patients with X-linked lissencephaly and subcortical band heterotopia.". Hum. Genet. 104 (4): 341–4. doi:10.1007/s004390050963. PMID 10369164.
- Gleeson JG, Lin PT, Flanagan LA, Walsh CA (1999). "Doublecortin is a microtubule-associated protein and is expressed widely by migrating neurons.". Neuron 23 (2): 257–71. doi:10.1016/S0896-6273(00)80778-3. PMID 10399933.
- Pilz DT, Kuc J, Matsumoto N; et al. (2000). "Subcortical band heterotopia in rare affected males can be caused by missense mutations in DCX (XLIS) or LIS1.". Hum. Mol. Genet. 8 (9): 1757–60. doi:10.1093/hmg/8.9.1757. PMID 10441340.
- Sakamoto M, Ono J, Okada S; et al. (2000). "Genetic alteration of the DCX gene in Japanese patients with subcortical laminar heterotopia or isolated lissencephaly sequence.". J. Hum. Genet. 45 (3): 167–70. doi:10.1007/s100380050204. PMID 10807542.
- Caspi M, Atlas R, Kantor A; et al. (2001). "Interaction between LIS1 and doublecortin, two lissencephaly gene products.". Hum. Mol. Genet. 9 (15): 2205–13. doi:10.1093/oxfordjournals.hmg.a018911. PMID 11001923.
- Matsumoto N, Leventer RJ, Kuc JA; et al. (2001). "Mutation analysis of the DCX gene and genotype/phenotype correlation in subcortical band heterotopia.". Eur. J. Hum. Genet. 9 (1): 5–12. doi:10.1038/sj.ejhg.5200548. PMID 11175293.
- Demelas L, Serra G, Conti M; et al. (2001). "Incomplete penetrance with normal MRI in a woman with germline mutation of the DCX gene.". Neurology 57 (2): 327–30. doi:10.1212/wnl.57.2.327. PMID 11468322.
- Friocourt G, Chafey P, Billuart P; et al. (2001). "Doublecortin interacts with mu subunits of clathrin adaptor complexes in the developing nervous system.". Mol. Cell. Neurosci. 18 (3): 307–19. doi:10.1006/mcne.2001.1022. PMID 11591131.
- Kato M, Kanai M, Soma O; et al. (2001). "Mutation of the doublecortin gene in male patients with double cortex syndrome: somatic mosaicism detected by hair root analysis.". Ann. Neurol. 50 (4): 547–51. doi:10.1002/ana.1231. PMID 11601509.
- des Portes V, Abaoub L, Joannard A; et al. (2002). "So-called 'cryptogenic' partial seizures resulting from a subtle cortical dysgenesis due to a doublecortin gene mutation.". Seizure : the journal of the British Epilepsy Association 11 (4): 273–7. doi:10.1053/seiz.2001.0607. PMID 12027577.
- Kizhatil K, Wu YX, Sen A, Bennett V (2002). "A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin.". J. Neurosci. 22 (18): 7948–58. PMID 12223548.
- D'Agostino MD, Bernasconi A, Das S; et al. (2002). "Subcortical band heterotopia (SBH) in males: clinical, imaging and genetic findings in comparison with females.". Brain 125 (Pt 11): 2507–22. doi:10.1093/brain/awf248. PMID 12390976.
- Meyer G, Perez-Garcia CG, Gleeson JG (2003). "Selective expression of doublecortin and LIS1 in developing human cortex suggests unique modes of neuronal movement.". Cereb. Cortex 12 (12): 1225–36. doi:10.1093/cercor/12.12.1225. PMID 12427674.
- Media related to doublecortin at Wikimedia Commons
- GeneReviews/NCBI/NIH/UW entry on DCX-Related Disorders
- OMIM entries on DCX-Related Disorders
- doublecortin protein at the US National Library of Medicine Medical Subject Headings (MeSH)
This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Doublecortin Provide feedback
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This tab holds annotation information from the InterPro database.
InterPro entry IPR003533
X-linked lissencephaly is a severe brain malformation affecting males. Recently it has been demonstrated that the doublecortin gene is implicated in this disorder [PUBMED:9489699]. Doublecortin was found to bind to the microtubule cytoskeleton. In vivo and in vitro assays show that Doublecortin stabilises microtubules and causes bundling [PUBMED:10441322]. Doublecortin is a basic protein with an iso-electric point of 10, typical of microtubule-binding proteins. However, its sequence contains no known microtubule-binding domain(s).
The detailed sequence analysis of Doublecortin and Doublecortin-like proteins allowed the identification of an evolutionarily conserved Doublecortin (DC) domain. This domain is found in the N terminus of proteins and consists of one or two tandemly repeated copies of an around 80 amino acids region. It has been suggested that the first DC domain of Doublecortin binds tubulin and enhances microtubule polymerisation [PUBMED:10749977].
Some proteins known to contain a DC domain are listed below:
- Doublecortin. It is required for neuronal migration [PUBMED:9489699]. A large number of point mutations in the human DCX gene leading to lissencephaly are located within the DC domains [PUBMED:10749977].
- Human serine/threonine-protein kinase DCAMKL1. It is a probable kinase that may be involved in a calcium-signaling pathway controling neuronal migration in the developing brain [PUBMED:10533048].
- Retinitis pigmentosa 1 protein. It could play a role in the differentiation of photoreceptor cells. Mutation in the human RP1 gene cause retinitis pigmentosa of type 1 [PUBMED:10401003].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||intracellular signal transduction (GO:0035556)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
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|Number in seed:||268|
|Number in full:||1347|
|Average length of the domain:||58.70 aa|
|Average identity of full alignment:||31 %|
|Average coverage of the sequence by the domain:||13.94 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||14|
|Download:||download the raw HMM for this family|
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the More....
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The tree is built by considering the taxonomic lineage of each sequence that has a match to this family. For each node in the resulting tree, we draw an arc in the sunburst. The radius of the arc, its distance from the root node at the centre of the sunburst, shows the taxonomic level ("superkingdom", "kingdom", etc). The length of the arc represents either the number of sequences represented at a given level, or the number of species that are found beneath the node in the tree. The weighting scheme can be changed using the sunburst controls.
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Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
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Since we reduce the species tree to only the eight main taxonomic levels, sequences that are mapped to the sub-species level in the tree would not normally be shown. Rather than leave out these species, we map them instead to their parent species. So, for example, for sequences belonging to one of the Vibrio cholerae sub-species in the NCBI taxonomy, we show them instead as belonging to the species Vibrio cholerae.
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The tree shows the occurrence of this domain across different species. More...
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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We use the NCBI species tree to group organisms according to their taxonomy and this forms the structure of the displayed tree. Note that in some cases the trees are too large (have too many nodes) to allow us to build an interactive tree, but in most cases you can still view the tree in a plain text, non-interactive representation. Those species which are represented in the seed alignment for this domain are highlighted.
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There are 2 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DCX domain has been found. There are 8 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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