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Search results 201 to 240 out of 240 for Dock2

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Type Details Score
Allele
Name: dedicator of cyto-kinesis 2; mutation 11, Bruce Beutler
Allele Type: Chemically induced (ENU)
Attribute String: Not Specified
Strain
Attribute String: chemically induced mutation, mutant strain, coisogenic
Allele
Name: dedicator of cyto-kinesis 2; mutation 9, Bruce Beutler
Allele Type: Chemically induced (ENU)
Attribute String: Not Specified
Strain
Attribute String: chemically induced mutation, mutant strain, coisogenic
Genotype
Symbol: Dock2/Dock2
Background: C57BL/6J-Dock2
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Dock2/Dock2
Background: C57BL/6J-Dock2
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Dock2/Dock2
Background: C57BL/6J-Dock2
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Dock2/Dock2
Background: C57BL/6J-Dock2
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Dock2/Dock2
Background: C57BL/6J-Dock2
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Dock2/Dock2
Background: C57BL/6J-Dock2
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Dock2/Dock2
Background: C57BL/6J-Dock2
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Dock2/Dock2
Background: C57BL/6J-Dock2
Zygosity: hm
Has Mutant Allele: true
Genotype
Symbol: Dock2/Dock2
Background: C57BL/6J-Dock2
Zygosity: hm
Has Mutant Allele: true
Protein Domain
Type: Family
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents DOCK2 (dedicator of cytokinesis 2). DOCK2 is involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. It activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. It may also participate in IL2 transcriptional activation via the activation of RAC2 [].
Publication
First Author: Komander D
Year: 2008
Journal: Mol Biol Cell
Title: An alpha-helical extension of the ELMO1 pleckstrin homology domain mediates direct interaction to DOCK180 and is critical in Rac signaling.
Volume: 19
Issue: 11
Pages: 4837-51
Publication
First Author: Wang J
Year: 2014
Journal: Int J Gynecol Cancer
Title: Elmo1 helps dock180 to regulate Rac1 activity and cell migration of ovarian cancer.
Volume: 24
Issue: 5
Pages: 844-50
Publication
First Author: Capala ME
Year: 2014
Journal: PLoS One
Title: ELMO1 is upregulated in AML CD34+ stem/progenitor cells, mediates chemotaxis and predicts poor prognosis in normal karyotype AML.
Volume: 9
Issue: 10
Pages: e111568
Publication  
First Author: Li H
Year: 2013
Journal: Nat Commun
Title: Association between Gαi2 and ELMO1/Dock180 connects chemokine signalling with Rac activation and metastasis.
Volume: 4
Pages: 1706
Protein Domain
Type: Family
Description: This entry represents engulfment and cell motility protein 1 (ELMO1) from vertebrates. ELMO1 is a scaffolding component of the Elmo-Dock complex. It interacts with DOCK180, which is essential for activation of Rac GTPase-dependent biological processes. Its C-terminal pleckstrin homology (PH) domain mediates direct interaction to DOCK180 and is critical in Rac signalling []. ELMO1 also interacts with DOCK2 and plays a role in controlling DOCK2 levels and DOCK2-dependent T cell migration in primary lymphocytes [, ]. ELMO1 has been linked to invasive phenotype of cancer cells [, , ].ELMO 1-3 are orthologues of the Caenorhabditis elegans ced-12, which is required for the engulfment of dying cells and cell migration []. They are cytoplasmic adaptor proteins that interact with DOCK family guanine nucleotide exchange factors (GEFs) to promote activation of the small GTPase Rac []. ELMO proteins interact with the SH3-domain of DOCKs via an SH3-binding site to enhance the GEF activity of DOCKs. Regulatory GTPases in the Ras superfamily employ a cycle of alternating GTP binding and hydrolysis, controlled by GEFs and GTPase-activating proteins (GAPs), as essential features of their actions in cells [, ].
Protein
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
Publication
First Author: Tajiri H
Year: 2017
Journal: Cell Rep
Title: Targeting Ras-Driven Cancer Cell Survival and Invasion through Selective Inhibition of DOCK1.
Volume: 19
Issue: 5
Pages: 969-980
Protein
Organism: Mus musculus/domesticus
Length: 193  
Fragment?: true
Publication
First Author: Yan D
Year: 2006
Journal: J Mol Biol
Title: An isoform of GTPase regulator DOCK4 localizes to the stereocilia in the inner ear and binds to harmonin (USH1C).
Volume: 357
Issue: 3
Pages: 755-64
Publication
First Author: Pierini R
Year: 2013
Journal: J Immunol
Title: ASC controls IFN-γ levels in an IL-18-dependent manner in caspase-1-deficient mice infected with Francisella novicida.
Volume: 191
Issue: 7
Pages: 3847-57
Publication  
First Author: Morino K
Year: 2023
Journal: Front Immunol
Title: Cholesterol sulfate limits neutrophil recruitment and gut inflammation during mucosal injury.
Volume: 14
Pages: 1131146
Publication
First Author: Gumienny TL
Year: 2001
Journal: Cell
Title: CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is required for phagocytosis and cell migration.
Volume: 107
Issue: 1
Pages: 27-41
Publication
First Author: Yasuda K
Year: 2014
Journal: PLoS One
Title: Interferon regulatory factor-5 deficiency ameliorates disease severity in the MRL/lpr mouse model of lupus in the absence of a mutation in DOCK2.
Volume: 9
Issue: 7
Pages: e103478
Publication
First Author: Kulkarni K
Year: 2011
Journal: J Biol Chem
Title: Multiple factors confer specific Cdc42 and Rac protein activation by dedicator of cytokinesis (DOCK) nucleotide exchange factors.
Volume: 286
Issue: 28
Pages: 25341-51
Publication
First Author: Thackray LB
Year: 2014
Journal: J Virol
Title: Interferon regulatory factor 5-dependent immune responses in the draining lymph node protect against West Nile virus infection.
Volume: 88
Issue: 19
Pages: 11007-21
Protein
Organism: Mus musculus/domesticus
Length: 727  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 741  
Fragment?: true
Publication
First Author: Bowzard JB
Year: 2007
Journal: J Biol Chem
Title: ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs.
Volume: 282
Issue: 24
Pages: 17568-80
Protein
Organism: Mus musculus/domesticus
Length: 1567  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 732  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1175  
Fragment?: false
Publication
First Author: Lu M
Year: 2005
Journal: Curr Biol
Title: A Steric-inhibition model for regulation of nucleotide exchange via the Dock180 family of GEFs.
Volume: 15
Issue: 4
Pages: 371-7
Publication
First Author: Gadea G
Year: 2014
Journal: Eur J Cell Biol
Title: Dock-family exchange factors in cell migration and disease.
Volume: 93
Issue: 10-12
Pages: 466-77
Protein
Organism: Mus musculus/domesticus
Length: 1828  
Fragment?: false
Publication
First Author: Côté JF
Year: 2002
Journal: J Cell Sci
Title: Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity.
Volume: 115
Issue: Pt 24
Pages: 4901-13