Search results for VAV2

Showing 19 results out of 49

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Protein (2 results from a total of 2)

Identifier: R-HSA-195012
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: P52735
Identifier: R-HSA-442307
Species: Homo sapiens
Compartment: cytosol
Primary external reference: UniProt: VAV2: P52735

Interactor (1 results from a total of 1)

Identifier: P52735-1
Species: Homo sapiens
Primary external reference: UniProt: P52735-1

Reaction (5 results from a total of 35)

Identifier: R-HSA-445085
Species: Homo sapiens
Compartment: cytosol
L1 crosslinking leads to the tyrosine phosphorylation and activation of VAV2. Tyr-172 in VAV2 binds to the DBL homology region autoinhibiting its GEF-activity. Tyrosine kinase src may phosphorylate this residue and relieve the autoinhibition.
Identifier: R-HSA-445064
Species: Homo sapiens
Compartment: cytosol
The small GTPase p21Rac1 is one of the important targets of VAV2 GEF activity. On L1 stimulation tyrosine phosphorylated VAV2, catalyses GDP/GTP exchange on Rac1.
Identifier: R-HSA-442291
Species: Homo sapiens
Compartment: cytosol
Members of the Vav family are guanine nucleotide exchange factors (GEFs) for Rho-family GTPases. Vav2 is a GEF for RhoA, RhoB and RhoG, and possibly Rac1 and Cdc42
Identifier: R-HSA-2424476
Species: Homo sapiens
Compartment: plasma membrane
Activated VAV2/3 act as guanine nucleotide exchange factors (GEFs) for RAC-1, catalysing the exchange of bound GDP for GTP.
Identifier: R-HSA-2424486
Species: Homo sapiens
Compartment: plasma membrane
VAV exists in an auto-inhibitory state, folded in such a way as to inhibit the GEF activity of its DH domain. This folding is mediated through binding of tyrosines in the acidic domain to the DH domain and through binding of the calponin homology (CH) domain to the C1 region. Activation of VAV may involve three events which relieve this auto-inhibition: phosphorylation of tyrosines in the acidic domain causes them to be displaced from the DH domain; binding of a ligand to the CH domain may cause it to release the C1 domain; binding of the PI3K product PIP3 to the PH domain may alter its conformation (Aghazadeh et al. 2000). VAV2/3 are phosphorylated on Y172/Y173 respectively in the acidic domain. This is mediated by SYK and Src-family tyrosine kinases (Deckert et al. 1996, Schuebel et al. 1998). Once activated, VAV2/VAV3 are involved in the activation of RAC1, PAK1, MEK and ERK.

Set (4 results from a total of 4)

Identifier: R-HSA-442284
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-2424458
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-2424465
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-430172
Species: Homo sapiens
Compartment: cytosol

Complex (3 results from a total of 3)

Identifier: R-HSA-442278
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-442290
Species: Homo sapiens
Compartment: cytosol
Identifier: R-HSA-3928532
Species: Homo sapiens
Compartment: plasma membrane

Pathway (4 results from a total of 4)

Identifier: R-HSA-445144
Species: Homo sapiens
Besides adhesive roles in cell cell interaction, L1 functions as a signal transducing receptor providing neurons with cues from their environment for axonal growth and guidance. L1 associates with beta1 integrins on the cell surface to induce a signaling pathway involving sequential activation of pp60csrc, Vav2 -GEF, Rac1, PAK1, MEK and ERK1/2. L1 stimulates cell migration and neurite outgrowth through the MAP kinases ERK1/2. CHL1 also associates with integrins and activates a MAPK signaling pathway via pp60c-src, MEK and ERK1/2.
L1 also binds the Sema3A receptor neuropilin1 and acts as an obligate coreceptor to mediate Sema3A induced growth cone collapse and axon repulsion. This repulsion can be converted to attraction by homophilic binding of L1 on an apposing cell in trans with L1 complexed with Neuropilin1 (NP1) in the responding neuron.
L1 also interacts with FGF receptor and activates PLC gamma and DAG, resulting in the production of arachidonic acid and subsequent opening of voltage-gated channels.
Identifier: R-HSA-9013149
Species: Homo sapiens
This pathway catalogues RAC1 guanine nucleotide exchange factors (GEFs), GTPase activator proteins (GAPs), GDP dissociation inhibitors (GDIs) and RAC1 effectors (reviewed by Payapilli and Malliri 2018). RAC1 is one of the three best characterized RHO GTPases, the other two being RHOA and CDC42. RAC1 regulates the cytoskeleton and the production of reactive oxygen species (ROS) (Acevedo and Gonzalez-Billault 2018) and is involved in cell adhesion and cell migration (Marei and Malliri 2017). RAC1 is involved in neuronal development (de Curtis et al. 2014). In neurons, RAC1 activity is regulated by synaptic activation and RAC1-mediated changes in actin cytoskeleton are implicated in dendritic spine morphogenesis, which plays a role in memory formation and learning (Tajeda-Simon 2015; Costa et al. 2020). RAC1 is involved in metabolic regulation of pancreatic islet β-cells and in diabetes pathophysiology (Kowluru 2017; Kowluru et al. 2020). RAC1-mediated activation of NOX2 contributes to mitochondrial damage and the development of retinopathy in patients with diabetes (Sahajpal et al. 2019). RAC1 is important for exercise and contraction-stimulated glucose uptake in skeletal muscles (Sylow et al. 2014). RAC1 plays an important role in the maintenance of intestinal barrier integrity under physiological conditions and during tissue repair after resolution of colitis. Toxins of many diarrhea-causing bacteria target RAC1 (Kotelevets and Chastre 2020). RAC1 is important for skin homeostasis and wound healing and is involved in the pathogenesis of psoriasis (Winge and Marinkovich 2019). RAC1 is essential to vascular homeostasis and chronically elevated RAC1 signaling contributes to vascular pathology (Marinkovic et al. 2015). RAC1 hyperactivation, mutation and copy-number gain are frequently observed in solid tumors (Zou et al. 2017; De et al. 2019; De et al. 2020; Cannon et al. 2020; Kotelevets and Chastre 2020).
Identifier: R-HSA-1306955
Species: Homo sapiens
Heterodimers of ERBB2 and ERBB3 are able to bind GRB7 (Fiddes et al. 1998) through phosphorylated tyrosine residues in the C-tail of ERBB3 (Y1199 and Y1262) (Fiddes et al. 1998), but the exact downstream signaling of this complex has not been elucidated. GRB7 can recruit SHC1 to the active ERBB2 complex, and contributes to ERBB2 signaling-induced RAS activation, which promotes cellular proliferation, but the exact mechanism has not been elucidated (Pradip et al. 2013). In addition, GRB7 can be phosphorylated by the integrin-activated PTK2 (FAK), leading to VAV2-dependent activation of RAC1 and promotion of cell migration. The exact mechanistic details of GRB7-induced RAC1 activation are not known (Pradip et al. 2013).
Identifier: R-HSA-5218920
Species: Homo sapiens
Compartment: cytosol, extracellular region, plasma membrane
The free radical nitric oxide (NO), produced by endothelial NO synthase (eNOS), is an important vasoactive substance in normal vascular biology and pathophysiology. It plays an important role in vascular functions such as vascular dilation and angiogenesis (Murohara et al. 1998, Ziche at al. 1997). NO has been reported to be a downstream mediator in the angiogenic response mediated by VEGF, but the mechanism by which NO promotes neovessel formation is not clear (Babaei & Stewart 2002). Persistent vasodilation and increase in vascular permeability in the existing vasculature is observed during the early steps of angiogenesis, suggesting that these hemodynamic changes are indispensable during an angiogenic processes. NO production by VEGF can occur either through the activation of PI3K or through a PLC-gamma dependent manner. Once activated both pathways converge on AKT phosphorylation of eNOS, releasing NO (Lin & Sessa 2006). VEGF also regulates vascular permeability by promoting VE-cadherin endocytosis at the cell surface through a VEGFR-2-Src-Vav2-Rac-PAK signalling axis.
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