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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Dedicator of cytokinesis 9

DOCK9, Zizimin1, dedicator of cytokinesis 9
novel thyroid transcript negatively regulated by thyroid stimulating hormone [RGD, Feb 2006] (from NCBI)
Top mentioned proteins: Rhodopsin, Cdc42, GEF, DOCK180, Akt
Papers on DOCK9
Variant c.2262A>C in DOCK9 Leads to Exon Skipping in Keratoconus Family.
New
Gajecka et al., Poznań, Poland. In Invest Ophthalmol Vis Sci, Jan 2016
Previously, we identified heterozygous single base-pair substitutions in DOCK9, IPO5, and STK24, showing concurrent 100% segregation with the affected phenotype in an Ecuadorian family.
Somatic amplifications and deletions in genome of papillary thyroid carcinomas.
New
Damante et al., Udine, Italy. In Endocrine, Nov 2015
Analysis of single aberrations according to the ATA risk grouping shows that amplifications containing PDE5A, GALNTL6, DHRS3, and DOCK9 genes are significantly more frequent in the intermediate/high risk group than in the low risk group.
Molecular Screening of Keratoconus Susceptibility Sequence Variants in VSX1, TGFBI, DOCK9, STK24, and IPO5 Genes in Polish Patients and Novel TGFBI Variant Identification.
New
Gajecka et al., Poznań, Poland. In Ophthalmic Genet, Sep 2015
The purpose of our study was to verify the role of VSX1, TGFBI, DOCK9, IPO5, and STK24 sequence variants in Polish KTCN patients.
Dock10, a Cdc42 and Rac1 GEF, induces loss of elongation, filopodia, and ruffles in cervical cancer epithelial HeLa cells.
Parrado et al., Cartagena, Spain. In Biol Open, 2014
Its homologs Dock9 and Dock11 are Cdc42 GEFs.
A Rac/Cdc42 exchange factor complex promotes formation of lateral filopodia and blood vessel lumen morphogenesis.
Mavria et al., Toronto, Canada. In Nat Commun, 2014
VEGF promotes interaction of DOCK4 with the CDC42 GEF DOCK9.
Insights into keratoconus from a genetic perspective.
Review
Vincent et al., Adelaide, Australia. In Clin Exp Optom, 2013
Family-based studies have recently led to the identification of the MIR184 gene for keratoconus with cataract and to the DOCK9 gene in a family with isolated keratoconus.
The Genetics of Keratoconus: A Review.
Liu et al., Durham, United States. In Reprod Syst Sex Disord, 2012
The genes implicated potentially include VSX1, miR-184, DOCK9, SOD1, RAB3GAP1, and HGF.
Novel mutation and three other sequence variants segregating with phenotype at keratoconus 13q32 susceptibility locus.
Gajecka et al., Poznań, Poland. In Eur J Hum Genet, 2012
Consequently, we have chosen eight positional candidate genes in this region: MBNL1, IPO5, FARP1, RNF113B, STK24, DOCK9, ZIC5 and ZIC2, and sequenced all of them in 51 individuals from Ecuadorian KTCN families and 105 matching controls.
In vivo fluorescence resonance energy transfer imaging reveals differential activation of Rho-family GTPases in glioblastoma cell invasion.
Matsuda et al., Kyoto, Japan. In J Cell Sci, 2012
We also studied the Cdc42-specific guanine nucleotide exchange factor Zizimin1 (also known as DOCK9) as a possible contributor to this spatially controlled activation of Rho-family GTPases, because it is known to play an essential role in the extension of neurites.
Multiple factors confer specific Cdc42 and Rac protein activation by dedicator of cytokinesis (DOCK) nucleotide exchange factors.
Barford et al., London, United Kingdom. In J Biol Chem, 2011
Although the molecular basis for DOCK(DHR2)-mediated GTPase activation has been elucidated through structures of a DOCK9(DHR2)-Cdc42 complex, the factors determining recognition of specific GTPases are unknown.
A minimal Rac activation domain in the unconventional guanine nucleotide exchange factor Dock180.
Erickson et al., Ithaca, United States. In Biochemistry, 2011
While extensive characterization of the Dbl family has been performed, less is known about how Dock180 family members act as GEFs, with only a single X-ray structure having recently been reported for the Dock9-Cdc42 complex.
Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor.
Impact
GeneRIF
Barford et al., London, United Kingdom. In Science, 2009
through structural analysis of DOCK9-Cdc42 complexes, we identify a nucleotide sensor within the alpha10 helix of the DHR2 domain that contributes to release of guanine diphosphate (GDP) and then to discharge of the activated GTP-bound Cdc42
Regulation of dendrite growth by the Cdc42 activator Zizimin1/Dock9 in hippocampal neurons.
GeneRIF
Katoh et al., Kyoto, Japan. In J Neurosci Res, 2009
Thus, these results suggest that Zizimin1 plays an important role in dendrite growth in hippocampal neurons through activation of Cdc42.
Snapshots form a big picture of guanine nucleotide exchange.
GeneRIF
Rittinger, London, United Kingdom. In Sci Signal, 2008
Studies indicate that that many of the mechanistic principles of the exchange process are conserved in the DOCK9-catalyzed reaction.
Identification of novel Smad2 and Smad3 associated proteins in response to TGF-beta1.
GeneRIF
Moses et al., New York City, United States. In J Cell Biochem, 2008
interaction between Smad2/3 and the Cdc42 guanine nucleotide exchange factor, Zizimin1, in response to TGF-beta1
Dock10, a novel CZH protein selectively induced by interleukin-4 in human B lymphocytes.
Parrado et al., Cartagena, Spain. In Mol Immunol, 2008
The Zizimin subfamily is composed of three members: Dock9, Dock10, and Dock11.
Specific recognition of Rac2 and Cdc42 by DOCK2 and DOCK9 guanine nucleotide exchange factors.
GeneRIF
Skowronski et al., New York City, United States. In J Biol Chem, 2008
DOCK2 and DOCK9 specifically recognize Rac2 and Cdc42 through their switch 1 as well as beta2-beta3 regions and the mode of recognition via switch 1 appears to be conserved among diverse Rac-specific DHR-2 GEFs
Zizimin1, a novel Cdc42 activator, reveals a new GEF domain for Rho proteins.
Impact
GeneRIF
Schwartz et al., Los Angeles, United States. In Nat Cell Biol, 2002
Sequence comparison combined with mutational analysis identified a new domain, which we named CZH2, that mediates direct interaction with Cdc42
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