HCSGD entry for RAC1

1. General information

Official gene symbolRAC1
Entrez ID5879
Gene full nameras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)
Other gene symbolsRac-1 TC-25 p21-Rac1
Links to Entrez GeneLinks to Entrez Gene

2. Neighbors in the network

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3. Gene ontology annotation

GO ID

GO term

Evidence

Category

GO:0000139Golgi membraneIEAcellular_component
GO:0001891Phagocytic cupIEAcellular_component
GO:0001934Positive regulation of protein phosphorylationIMPbiological_process
GO:0002093Auditory receptor cell morphogenesisIEAbiological_process
GO:0002551Mast cell chemotaxisIEAbiological_process
GO:0003382Epithelial cell morphogenesisIEAbiological_process
GO:0003924GTPase activityTASmolecular_function
GO:0005515Protein bindingIPImolecular_function
GO:0005525GTP bindingIDAmolecular_function
GO:0005802Trans-Golgi networkIDAcellular_component
GO:0005829CytosolISS TAScellular_component
GO:0005886Plasma membraneTAScellular_component
GO:0006928Cellular component movementTASbiological_process
GO:0006954Inflammatory responseTASbiological_process
GO:0006972Hyperosmotic responseIEAbiological_process
GO:0007155Cell adhesionTASbiological_process
GO:0007160Cell-matrix adhesionNASbiological_process
GO:0007264Small GTPase mediated signal transductionIEAbiological_process
GO:0007411Axon guidanceTASbiological_process
GO:0007596Blood coagulationTASbiological_process
GO:0008283Cell proliferationIEAbiological_process
GO:0009611Response to woundingTASbiological_process
GO:0009653Anatomical structure morphogenesisTASbiological_process
GO:0010310Regulation of hydrogen peroxide metabolic processTASbiological_process
GO:0010592Positive regulation of lamellipodium assemblyIDAbiological_process
GO:0016020MembraneISScellular_component
GO:0016032Viral processTASbiological_process
GO:0017137Rab GTPase bindingIEAmolecular_function
GO:0019897Extrinsic component of plasma membraneIEAcellular_component
GO:0019899Enzyme bindingIPImolecular_function
GO:0019901Protein kinase bindingIEAmolecular_function
GO:0021799Cerebral cortex radially oriented cell migrationIEAbiological_process
GO:0021831Embryonic olfactory bulb interneuron precursor migrationIEAbiological_process
GO:0030027LamellipodiumIEAcellular_component
GO:0030032Lamellipodium assemblyIMPbiological_process
GO:0030036Actin cytoskeleton organizationIGIbiological_process
GO:0030041Actin filament polymerizationTASbiological_process
GO:0030168Platelet activationTASbiological_process
GO:0030334Regulation of cell migrationIMPbiological_process
GO:0030742GTP-dependent protein bindingIEAmolecular_function
GO:0030838Positive regulation of actin filament polymerizationIEAbiological_process
GO:0031295T cell costimulationTASbiological_process
GO:0031529Ruffle organizationIDA TASbiological_process
GO:0031996Thioesterase bindingIPImolecular_function
GO:0032587Ruffle membraneIEAcellular_component
GO:0032707Negative regulation of interleukin-23 productionIDAbiological_process
GO:0034446Substrate adhesion-dependent cell spreadingIEAbiological_process
GO:0035025Positive regulation of Rho protein signal transductionTASbiological_process
GO:0035556Intracellular signal transductionTASbiological_process
GO:0038095Fc-epsilon receptor signaling pathwayTASbiological_process
GO:0038096Fc-gamma receptor signaling pathway involved in phagocytosisTASbiological_process
GO:0042470MelanosomeIEAcellular_component
GO:0043065Positive regulation of apoptotic processTASbiological_process
GO:0043552Positive regulation of phosphatidylinositol 3-kinase activityIEAbiological_process
GO:0043652Engulfment of apoptotic cellIEAbiological_process
GO:0045087Innate immune responseTASbiological_process
GO:0045216Cell-cell junction organizationIEAbiological_process
GO:0045453Bone resorptionIEAbiological_process
GO:0045740Positive regulation of DNA replicationIEAbiological_process
GO:0048011Neurotrophin TRK receptor signaling pathwayTASbiological_process
GO:0048261Negative regulation of receptor-mediated endocytosisTASbiological_process
GO:0048532Anatomical structure arrangementIEAbiological_process
GO:0048813Dendrite morphogenesisIEAbiological_process
GO:0048870Cell motilityIDAbiological_process
GO:0050690Regulation of defense response to virus by virusTASbiological_process
GO:0051022Rho GDP-dissociation inhibitor bindingISSmolecular_function
GO:0051668Localization within membraneIMPbiological_process
GO:0060071Wnt signaling pathway, planar cell polarity pathwayIEAbiological_process
GO:0060263Regulation of respiratory burstIDAbiological_process
GO:0071526Semaphorin-plexin signaling pathwayISSbiological_process
GO:0071542Dopaminergic neuron differentiationIEAbiological_process
GO:0090103Cochlea morphogenesisIEAbiological_process
GO:0097178Ruffle assemblyIEAbiological_process
GO:0097190Apoptotic signaling pathwayTASbiological_process
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4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.95337503890.16061757150.99999024730.7737216508

  • Individual experiment result
    ( "-" represent NA in the specific microarray platform )

Data sourceUp or downLog fold change
GSE11954Down-0.2324529422
GSE13712_SHEARUp0.0828306686
GSE13712_STATICDown-0.0161509559
GSE19018Up0.1225895841
GSE19899_A1Down-0.0619381030
GSE19899_A2Up0.1285821931
PubMed_21979375_A1Down-0.5917276843
PubMed_21979375_A2Down-0.2332310640
GSE35957Up0.0165209013
GSE36640Down-0.1336450476
GSE54402Up0.0061844729
GSE9593Up0.1401845582
GSE43922Down-0.0799793632
GSE24585Up0.0310950403
GSE37065Down-0.0356272000
GSE28863_A1Up0.1052561421
GSE28863_A2Down-0.0717584579
GSE28863_A3Down-0.4933873608
GSE28863_A4Down-0.0425064227
GSE48662Down-0.4837576034

5. Regulation relationships with compounds/drugs/microRNAs

  • Compounds

Not regulated by compounds

  • Drugs

Name

Drug

Accession number

Guanosine-5'-DiphosphateDB04315 EXPT01573
DextromethorphanDB00514 APRD00655

  • MicroRNAs

  • mirTarBase

MiRNA_name

mirBase ID

miRTarBase ID

Experiment

Support type

References (Pubmed ID)

hsa-miR-142-3pMIMAT0000434MIRT006370GFP reporter assayFunctional MTI21482222
hsa-miR-122-5pMIMAT0000421MIRT000663Luciferase reporter assay//Functional MTI19935707
hsa-miR-194-5pMIMAT0000460MIRT005890Luciferase reporter assay//qRT-PCR//Western blotFunctional MTI20979124
hsa-miR-155-5pMIMAT0000646MIRT020715Reporter assay;OtherNon-Functional MTI20584899
hsa-miR-101-3pMIMAT0000099MIRT027282SequencingFunctional MTI (Weak)20371350
hsa-miR-652-3pMIMAT0003322MIRT039481CLASHFunctional MTI (Weak)23622248
hsa-miR-30c-5pMIMAT0000244MIRT047987CLASHFunctional MTI (Weak)23622248
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  • mirRecord
No target information from mirRecord

6. Text-mining results about the gene

Gene occurances in abstracts of cellular senescence-associated articles: 11 abstracts the gene occurs.


PubMed ID of the article

Sentenece the gene occurs

26658759The Rho family GTPases Rac1 and Cdc42 were activated in senescent cells, and simvastatin reduced both activities
26658759Further, geranylgeranyl transferase, Rac1 or Cdc42 depletion reduced IL-6 secretion by senescent cells
24583638We also show that oncogenic Ras-induced ROS are produced in a Rac1 and NADPH oxidase (Nox4)-dependent manner
24379346In addition, 1-deoxysphinganine altered cytoskeleton dynamics, resulting in intracellular accumulation of filamentous actin and activation of the Rho family GTPase Rac1
22335598Concomitantly, translocation of Rac1 to the plasma membrane, which leads to the activation of NADPH oxidases and generation of ROS, was significantly attenuated
18195103As a direct consequence, both Akt and Rac1 are hyperactivated, leading to cytoskeletal rearrangements and decreased endothelial cell motility, e
17032649Rac1 GTPase regulates cell genomic stability and senescence
17032649The Rho family small GTPase Rac1 has been shown to play multiple roles in cell regulation, including actin cytoskeleton organization, transcriptional activation, microtubule dynamics, and endocytosis
17032649Here, we report a novel role of Rac1 in regulating genomic stability and cell senescence
17032649We observed in primary mouse embryonic fibroblasts that deletion of rac1 by gene targeting, as well as expression of the constitutively active Rac1 mutant L61Rac1, led to decreased cell growth that was associated with altered cell cycle progression at both G(1)/S and G(2)/M phases, increased apoptosis, and premature senescence
17032649The senescence induction by either loss or gain of Rac1 activity was due at least in part to an increase in cellular reactive oxygen species (ROS)
17032649Furthermore, the Rac1-regulated ROS production and senescence correlated with the extent of DNA damage in the Rac1(-/-) and L61Rac1 cells
17032649Finally, phospho-Ser(15) p53 was significantly increased in L61Rac1 and Rac1(-/-) cells, and genetic deletion of p53 from these cells readily reversed the senescence phenotype, indicating that Rac1 is functionally dependent on p53 in regulating cell senescence
17032649Taken together, our results show that Rac1 activity serves as a regulator of cell senescence through modulation of cellular ROS, genomic stability, and p53 activity
16786104To investigate the role and mechanism of Rac1 protein in the process of the human umbilical vein endothelial cell (HUVEC) senescence, we used hypoxia as a model for modulating HUVECs entering replicative senescence in vitro
16786104Accompanied with these changes, the expression of activated Rac1 increased obviously in cells after hypoxia
16786104All these observations suggested that endothelial senescence could be induced by continued hypoxia and it might correlate with the activity of Rac1
16786104To further define the relationship between Rac1 and HUVEC senescence, HUVECs were transiently infected with the constitutively active form of Rac1 (V12Rac1) or dominant negative form of Rac1 (N17Rac1) using retrovirus vector pLNCX-V12Rac1 or pLNCX-N17Rac1
16786104We observed the changes of these three kinds of HUVECs (HUVECs, N17Rac1-HUVECs, V12Rac1-HUVECs) after hypoxia for 48 h and 96 h, the expression and localization of serum response factor (SRF), which is one of the downstream signal molecules of Rac1, were also investigated
16786104All the results identified that the activation of Rac1 might accelerate HUVEC senescence induced by hypoxia and that inactivation of Rac1 could partly block the cell senescence
16786104To further investigate the mechanism of HUVEC senescence induced by Rac1, we detected the expression of total SRF (tSRF) and nuclear SRF (nSRF) in these three kinds of HUVECs by immunofluorescent analysis and Western blot assay after hypoxia
16786104These results suggest that activation of Rac1 accelerates endothelial cell senescence and inhibition of Rac1 activity prevents HUVECs from entering senescence induced by hypoxia, while the nuclear translocation of SRF regulated by Rac1 might play an important role in the process of senescence
16510591Phosphorylation of ezrin by cyclin-dependent kinase 5 induces the release of Rho GDP dissociation inhibitor to inhibit Rac1 activity in senescent cells
16510591The release of Rho-GDI results in increased interaction with Rac1 GTPase and inhibition of Rac1 GTPase activity
15263006Moreover, the Rho GTPases Rac1 and Cdc42 were found to be highly activated in senescent cells
15263006Activated Rac1 and Cdc42 directly interacted with caveolin-1 in senescent cells
15024070Cellular senescence requires CDK5 repression of Rac1 activity
15024070The increased activity of CDK5 further reduces GTPase Rac1 activity and Pak activation
15024070The repression of the activity of the GTPase Rac1 by CDK5 is required for expression of the senescent phenotype
15024070CDK5 regulation of Rac1 activity is necessary for actin polymerization accompanying senescent morphology in response to expression of pRb, activated Ras, or continuous passage
15024070These results point to a unique, nonneuronal role for CDK5 in regulation of Rac1 activity in senescence, illuminating the mechanisms underlying induction of senescence and the senescent shape change
11795508Perinuclear expression of Rac1 was prominent in the HDF cells and V12C40 expresser; however, in the V12S35 expresser, translocation of Rac1 from perinucleus to nucleus and strong expression of RhoA were obvious
11795508In summary, the H-ras double mutant expressers induced premature senescence through the MEK pathway, accompanied by nuclear accumulation of actin and Rac1 proteins, cytoplasmic retention of p-Erk1/2, and marked induction of RhoA expression, suggesting the translocational inefficiency of the intracellular proteins in the senescent HDF cells
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