GTPases, genome, actin: A hidden story in DNA damage response and repair mechanisms
Tài liệu tham khảo
Aguilera, 2008, Genome instability: a mechanistic view of its causes and consequences, Nat. Rev. Genet., 9, 204, 10.1038/nrg2268
Hanna, 2013, Signaling networks of Rho GTPases in cell motility, Cell. Signal., 25, 1955, 10.1016/j.cellsig.2013.04.009
Ueyama, 2019, Rho-family small GTPases: from highly polarized sensory neurons to cancer cells, Cells, 8, 92, 10.3390/cells8020092
Haga, 2016, Rho GTPases: Regulation and roles in cancer cell biology, Small GTPases, 7, 207, 10.1080/21541248.2016.1232583
Stankiewicz, 2014, Rho family GTPases: key players in neuronal development, neuronal survival, and neurodegeneration, Front. Cell. Neurosci., 8, 314, 10.3389/fncel.2014.00314
Tybulewicz, 2009, Rho family GTPases and their regulators in lymphocytes, Nat. Rev. Immunol., 9, 630, 10.1038/nri2606
Bos, 2007, GEFs and GAPs: critical elements in the control of small g proteins, Cell., 865, 10.1016/j.cell.2007.05.018
Colicelli, 2004, Human RAS superfamily proteins and related GTPases, Sci. STKE, 2004, 10.1126/stke.2502004re13
Huret, 2013, Atlas of genetics and cytogenetics in oncology and haematology in 2013, Nucl. Acids Res., 41
Angeloni, 2007, Molecular analysis of deletions in human chromosome 3p21 and the role of resident cancer genes in disease, Briefings Funct. Genom. Proteom., 6, 19, 10.1093/bfgp/elm007
Chromosome Disorder Library - Chromosome Disorder Outreach, Inc., (n.d.). https://chromodisorder.org/library/ (accessed December 1, 2020).
Wheeler, 2004, Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility, Exp. Cell Res., 301, 43, 10.1016/j.yexcr.2004.08.012
Ju, 2018, Rhob: Team oncogene or team tumor suppressor?, Genes (Basel), 9, 10.3390/genes9020067
Schaefer, 2014, Toward understanding RhoGTPase specificity: structure, function and local activation, Small GTPases, 5, 10.4161/21541248.2014.968004
Svensmark, 2019, Rho GTPases in cancer: friend or foe?, Oncogene, 10.1038/s41388-019-0963-7
Wennerberg, 2004, Rho-family GTPases: it’s not only Rac and Rho (and I like it), J. Cell. Sci., 117, 10.1242/jcs.01118
Olson, 2018, Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors, Small GTPases, 9, 203, 10.1080/21541248.2016.1218407
Ridley, 2013, RhoA, RhoB and RhoC have different roles in cancer cell migration, J. Microsc., 251, 242, 10.1111/jmi.12025
Mokady, 2015, RhoGTPases – a novel link between cytoskeleton organization and cisplatin resistance, Drug Resist. Updat., 19, 22, 10.1016/j.drup.2015.01.001
Matos, 2000, Small GTPase Rac1: structure, localization, and expression of the human gene, Biochem. Biophys. Res. Commun., 277, 741, 10.1006/bbrc.2000.3743
Courjal, 1997, Structure and chromosomal assignment to 22q12 and 17qter of the ras- related Rac2 and Rac3 human genes, Genomics, 44, 242, 10.1006/geno.1997.4871
Haataja, 1997, Characterization of RAC3, a novel member of the Rho family, J. Biol. Chem., 272, 20384, 10.1074/jbc.272.33.20384
Jeon, 1995, A variant Ewing’s sarcoma translocation (7;22) fuses the EWS gene to the ETS gene ETV1, Oncogene, 10, 1229
Thompson, 1994, Clonal chromosome abnormalities in 54 cases of ovarian carcinoma, Cancer Genet. Cytogenet., 73, 33, 10.1016/0165-4608(94)90179-1
Bardi, 1995, Karyotypic characterization of colorectal adenocarcinomas, Genes. Chromosom. Cancer, 12, 97, 10.1002/gcc.2870120204
Rao, 1995, Cytogenetics of gastric and esophageal adenocarcinomas 3q deletion as a possible primary chromosomal change, Cancer Genet. Cytogenet., 81, 139, 10.1016/0165-4608(94)00113-P
Bardi, 1993, Karyotypic abnormalities in tumours of the pancreas, Br. J. Cancer, 67, 1106, 10.1038/bjc.1993.203
Mertens, 1995, Cytogenetic findings in malignant peripheral nerve sheath tumors, Int. J. Cancer, 61, 793, 10.1002/ijc.2910610609
Nagata, 1999, Karyotypic analyses of hepatoblastoma: report of two cases and review of the literature suggesting chromosomal loci responsible for the pathogenesis of this disease, Cancer Genet. Cytogenet., 114, 42, 10.1016/S0165-4608(99)00033-3
Gebhart, 1998, Pattern of genomic imbalances in oral squamous cell carcinomas with and without an increased copy number of 11q13, Int. J. Oncol., 12, 1151
Gogusev, 1999, Detection of DNA copy number changes in human endometriosis by comparative genomic hybridization, Hum. Genet., 105, 444, 10.1007/s004399900174
Pai, 2010, Rac GTPases in human diseases, Dis. Markers, 29, 177, 10.1155/2010/380291
Hodge, 2016, Regulating rho GTPases and their regulators, Nat. Rev. Mol. Cell Biol., 17, 496, 10.1038/nrm.2016.67
Del Mar Maldonado, 2018, Targeting rac and Cdc42 GT pases in cancer, Cancer Res., 78, 3101, 10.1158/0008-5472.CAN-18-0619
Jansen, 2018, Paving the Rho in cancer metastasis: rho GTPases and beyond, Pharmacol. Ther., 183, 1, 10.1016/j.pharmthera.2017.09.002
De, 2019, RAC1 takes the lead in solid tumors, Cells, 8, 382, 10.3390/cells8050382
Cardama, 2018, Relevance of small GTPase Rac1 pathway in drug and radio-resistance mechanisms: opportunities in cancer therapeutics, Crit. Rev. Oncol. Hematol., 124, 29, 10.1016/j.critrevonc.2018.01.012
Zhang, 1998, Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA, J. Biol. Chem., 273, 8776, 10.1074/jbc.273.15.8776
Takenouchi, 2016, Further evidence of a mutation in CDC42 as a cause of a recognizable syndromic form of thrombocytopenia, Am. J. Med. Genet. Part A, 170, 852, 10.1002/ajmg.a.37526
Motokawa, 2018, A hot-spot mutation in CDC42 (p.Tyr64Cys) and novel phenotypes in the third patient with Takenouchi-Kosaki syndrome, J. Hum. Genet., 63, 387, 10.1038/s10038-017-0396-5
Takenouchi, 2015, Macrothrombocytopenia and developmental delay with a de novo CDC42 mutation: yet another locus for thrombocytopenia and developmental delay, Am. J. Med. Genet. Part A, 167, 2822, 10.1002/ajmg.a.37275
Uehara, 2019, Pathogenetic basis of Takenouchi-Kosaki syndrome: electron microscopy study using platelets in patients and functional studies in a Caenorhabditis elegans model, Sci. Rep., 9, 10.1038/s41598-019-40988-7
He, 2015, Regulation and functional significance of CDC42 alternative splicing in ovarian cancer, Oncotarget, 6, 29651, 10.18632/oncotarget.4865
Wirth, 2013, Dual lipidation of the brain-specific Cdc42 isoform regulates its functional properties, Biochem. J., 456, 311, 10.1042/BJ20130788
Endo, 2020, The two splice variant forms of Cdc42 exert distinct and essential functions in neurogenesis, J. Biol. Chem., 295, 4498, 10.1074/jbc.RA119.011837
Boureux, 2007, Evolution of the rho family of ras-like GTPases in eukaryotes, Mol. Biol. Evol., 24, 203, 10.1093/molbev/msl145
Martinelli, 2018, Functional dysregulation of CDC42 causes diverse developmental phenotypes, Am. J. Hum. Genet., 102, 309, 10.1016/j.ajhg.2017.12.015
Cotteret, 2002, The evolutionary history of effectors downstream of Cdc42 and Rac, Genome Biol., 3, 10.1186/gb-2002-3-2-reviews0002
Watson, 2017, Cdc42 in actin dynamics: an ordered pathway governed by complex equilibria and directional effector handover, Small GTPases, 8, 237, 10.1080/21541248.2016.1215657
Etienne-Manneville, 2004, Cdc42 - the centre of polarity, J. Cell. Sci., 117, 1291, 10.1242/jcs.01115
Ridley, 2006, Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking, Trends Cell Biol., 16, 522, 10.1016/j.tcb.2006.08.006
Chuang, 1997, The small GTPase Cdc42 initiates an apoptotic signaling pathway in Jurkat T lymphocytes, Mol. Biol. Cell, 8, 1687, 10.1091/mbc.8.9.1687
Wang, 2007, Cdc42 GTPase-activating protein deficiency promotes genomic instability and premature aging-like phenotypes, Proc. Natl. Acad. Sci. U. S. A., 104, 1248, 10.1073/pnas.0609149104
Lawson, 2018, Rho GTPase signaling complexes in cell migration and invasion, J. Cell Biol., 217, 447, 10.1083/jcb.201612069
Debidda, 2006, Rac1 GTPase regulates cell genomic stability and senescence, J. Biol. Chem., 281, 38519, 10.1074/jbc.M604607200
Shi, 2016, Rac1-mediated DNA damage and inflammation promote Nf2 tumorigenesis but also limit cell-cycle progression, Dev. Cell, 10.1016/j.devcel.2016.09.027
Ito, 2014, A crucial role for CDC42 in senescence-associated inflammation and atherosclerosis, PLoS One, 10.1371/journal.pone.0102186
Umbayev, 2018, Elevated levels of the small GTPase Cdc42 induces senescence in male rat mesenchymal stem cells, Biogerontology, 10.1007/s10522-018-9757-5
Kümper, 2016, Rho-associated kinase (ROCK) function is essential for cell cycle progression, senescence and tumorigenesis, Elife, 5, 10.7554/eLife.12203
Park, 2007, Inhibitory role of RhoA on senescence-like growth arrest by a mechanism involving modulation of phosphatase activity, FEBS Lett., 10.1016/j.febslet.2007.07.007
Venkatesh, 2011, RhoA-mediated signaling in notch-induced senescence-like growth arrest and endothelial barrier dysfunction, Arterioscler. Thromb. Vasc. Biol., 10.1161/ATVBAHA.110.221945
Von Zglinicki, 2005, Human cell senescence as a DNA damage response, Mech. Ageing Dev.
Chen, 2007, DNA damage, cellular senescence and organismal ageing: causal or correlative?, Nucleic Acids Res., 10.1093/nar/gkm681
Martin, 2016, Spatio-temporal co-ordination of RhoA, Rac1 and Cdc42 activation during prototypical edge protrusion and retraction dynamics, Sci. Rep., 6, 10.1038/srep21901
Navarro-Lérida, 2015, Rac1 nucleocytoplasmic shuttling drives nuclear shape changes and tumor invasion, Dev. Cell, 32, 318, 10.1016/j.devcel.2014.12.019
Michaelson, 2008, Rac1 accumulates in the nucleus during the G2 phase of the cell cycle and promotes cell division, J. Cell Biol., 10.1083/jcb.200801047
Dubash, 2011, The small GTPase RhoA localizes to the nucleus and is activated by Net1 and DNA damage signals, PLoS One, 6, e17380, 10.1371/journal.pone.0017380
Sandrock, 2010, The nuclear import of the small GTPase Rac1 is mediated by the direct interaction with karyopherin α2, Traffic, 10.1111/j.1600-0854.2009.01015.x
Hurst, 2019, Nuclear actin and actin-binding proteins in DNA repair, Trends Cell Biol., 29, 462, 10.1016/j.tcb.2019.02.010
Ohnishi, 1963, Extraktion eines dem aktin ähnlichen proteins aus dem zellkern des kalbsthymus, J. Biochem., 54, 298, 10.1093/oxfordjournals.jbchem.a127789
Ishikawa, 1969, Formation of arrowhead complexes with heavy meromyosin in a variety of cell types, J. Cell Biol., 43, 312, 10.1083/jcb.43.2.312
Jockusch, 1971, Synthesis and some properties of an actin-like nuclear protein in the slime mold Physarum polycephalum, J. Bacteriol., 108, 705, 10.1128/jb.108.2.705-714.1971
Pederson, 2002, Actin in the nucleus: what form and what for?, J. Struct. Biol., 140, 3, 10.1016/S1047-8477(02)00528-2
Kristó, 2016, Actin, actin-binding proteins, and actin-related proteins in the nucleus, Histochem. Cell Biol., 145, 373, 10.1007/s00418-015-1400-9
Belin, 2015, DNA damage induces nuclear actin filament assembly by Formin-2 and Spire-1/2 that promotes efficient DNA repair, Elife, 4, e07735, 10.7554/eLife.07735
Bajusz, 2018, Nuclear actin: ancient clue to evolution in eukaryotes?, Histochem. Cell Biol., 150, 235, 10.1007/s00418-018-1693-6
Le, 2016, Mechanical regulation of transcription controls Polycomb-mediated gene silencing during lineage commitment, Nat. Cell Biol., 18, 864, 10.1038/ncb3387
Obrdlik, 2011, The F-actin severing protein cofilin-1 is required for RNA polymerase II transcription elongation, Nucleus, 2, 72, 10.4161/nucl.14508
Baarlink, 2017, A transient pool of nuclear F-actin at mitotic exit controls chromatin organization, Nat. Cell Biol., 19, 1389, 10.1038/ncb3641
de Leeuw, 2018, Nuclear Lamins: Thin Filaments with Major Functions, Trends Cell Biol., 28, 34, 10.1016/j.tcb.2017.08.004
Percipalle, 2019, Cytoskeletal proteins in the cell nucleus: a special nuclear actin perspective, Mol. Biol. Cell, 30, 1781, 10.1091/mbc.E18-10-0645
Wei, 2020, Nuclear actin regulates inducible transcription by enhancing RNA polymerase II clustering, Sci. Adv., 6, eaay6515, 10.1126/sciadv.aay6515
Fritz, 2015, Rho GTPases: novel players in the regulation of the DNA damage response?, Biomolecules, 5, 2417, 10.3390/biom5042417
Guerra, 2008, A bacterial cytotoxin identifies the RhoA exchange factor Net1 as a key effector in the response to DNA damage, PLoS One, 3, e2254, 10.1371/journal.pone.0002254
Mamouni, 2014, RhoB promotes γH2AX dephosphorylation and DNA double-strand break repair, Mol. Cell. Biol., 34, 3144, 10.1128/MCB.01525-13
Sahai, 2001, Cross-talk between Ras and Rho signalling pathways in transformation favours proliferation and increased motility, EMBO J., 20, 755, 10.1093/emboj/20.4.755
Luo, 2014, 8-Oxoguanine DNA glycosylase-1-mediated DNA repair is associated with Rho GTPase activation and α-smooth muscle actin polymerization, Free Radic. Biol. Med., 73, 430, 10.1016/j.freeradbiomed.2014.03.030
Pranatharthi, 2019, RhoC regulates radioresistance via crosstalk of ROCK2 with the DNA repair machinery in cervical cancer, J. Exp. Clin. Cancer Res., 38, 10.1186/s13046-019-1385-7
Osaki, 2016, Modulation of RhoA GTPase activity sensitizes human cervix carcinoma cells to γ -radiation by attenuating DNA repair pathways, Oxid. Med. Cell. Longev., 2016, 1, 10.1155/2016/6012642
Seifermann, 2017, Oxidatively generated base modifications in DNA: not only carcinogenic risk factor but also regulatory mark?, Free Radic. Biol. Med., 107, 258, 10.1016/j.freeradbiomed.2016.11.018
Sharma, 2014, The role of Rho GTPase in cell stiffness and cisplatin resistance in ovarian cancer cells, Integr. Biol. (U.K.), 6, 611, 10.1039/C3IB40246K
Sharma, 2012, Correlative nanomechanical profiling with super-resolution F-actin imaging reveals novel insights into mechanisms of cisplatin resistance in ovarian cancer cells, Nanomed. Nanotechnol. Biol. Med., 8, 757, 10.1016/j.nano.2011.09.015
Benedetti, 2013, The nuclear factor kB family member relB facilitates apoptosis of renal epithelial cells caused by cisplatin/tumor necrosis factor a synergy by suppressing an epithelial to mesenchymal transition-like phenotypic switchs, Mol. Pharmacol., 84, 128, 10.1124/mol.112.084053
Espinha, 2016, Inhibition of the RhoA GTPase activity increases sensitivity of melanoma cells to UV radiation effects, Oxid. Med. Cell. Longev., 2016, 10.1155/2016/2696952
Magalhaes, 2020, Exoenzyme C3 transferase lowers actin cytoskeleton dynamics, genomic stability and survival of malignant melanoma cells under UV-light stress, J. Photochem. Photobiol. B Biol., 209, 111947, 10.1016/j.jphotobiol.2020.111947
Magalhaes, 2020, RHOAming through the nucleotide excision repair pathway as a mechanism of cellular response against the effects of UV radiation, Front. Cell Dev. Biol., 8, 816, 10.3389/fcell.2020.00816
Bhowmick, 2003, TGF-β-induced RhoA and p160ROCK activation is involved in the inhibition of Cdc25A with resultant cell-cycle arrest, Proc. Natl. Acad. Sci. U. S. A., 100, 15548, 10.1073/pnas.2536483100
Zheng, 2019, TGF beta promotes repair of bulky DNA damage through increased ERCC1/XPF and ERCC1/XPA interaction, Carcinogenesis, 40, 580, 10.1093/carcin/bgy156
Chircop, 2014, Rho GTPases as regulators of mitosis and cytokinesis in mammalian cells, Small GTPases, 5, 10.4161/sgtp.29770
Zhang, 2009, RhoA regulates G1-S progression of gastric cancer cells by modulation of multiple INK4 family tumor suppressors, Mol. Cancer Res., 7, 570, 10.1158/1541-7786.MCR-08-0248
Lawson, 2016, Rho GTPase transcriptome analysis reveals oncogenic roles for rho GTPase-activating proteins in basal-like breast cancers, Cancer Res., 76, 3826, 10.1158/0008-5472.CAN-15-2923
Chang, 2015, The actin depolymerizing factor (ADF)/Cofilin signaling pathway and DNA damage responses in cancer, Int. J. Mol. Sci., 16, 4095, 10.3390/ijms16024095
Dias Gomes, 2019, Polarity signaling ensures epidermal homeostasis by coupling cellular mechanics and genomic integrity, Nat. Commun., 10, 10.1038/s41467-019-11325-3
Arsic, 2017, The p53 isoform delta133p53β regulates cancer cell apoptosis in a RhoB-dependent manner, PLoS One, 12
Mizuarai, 2006, Mutant p53 induces the GEF-H1 oncogene, a guanine nucleotide exchange factor-H1 for RhoA, resulting in accelerated cell proliferation in tumor cells, Cancer Res., 66, 6319, 10.1158/0008-5472.CAN-05-4629
Krendel, 2002, Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton, Nat. Cell Biol., 4, 294, 10.1038/ncb773
Spiering, 2011, Dynamics of the Rho-family small GTPases in actin regulation and motility, Cell Adh. Migr., 5, 170, 10.4161/cam.5.2.14403
Thumkeo, 2013, Physiological roles of rho and rho effectors in mammals, Eur. J. Cell Biol., 92, 303, 10.1016/j.ejcb.2013.09.002
Julian, 2014, Rho-associated coiled-coil containing kinases (ROCK), structure, regulation, and functions, Small GTPases, 5, 10.4161/sgtp.29846
Zhou, 2018, The RhoA/ROCK pathway mediates high glucose-induced cardiomyocyte apoptosis via oxidative stress, JNK, and p38MAPK pathways, Diabetes Metab. Res. Rev., 34, e3022, 10.1002/dmrr.3022
Salhia, 2008, The guanine nucleotide exchange factors trio, Ect2, and Vav3 mediate the invasive behavior of glioblastoma, Am. J. Pathol., 173, 1828, 10.2353/ajpath.2008.080043
Herraiz, 2016, Reactivation of p53 by a cytoskeletal sensor to control the balance between DNA damage and tumor dissemination, J. Natl. Cancer Inst., 108, 10.1093/jnci/djv289
Lefort, 2007, Notch1 is a p53 target gene involved in human keratinocyte tumor suppression through negative regulation of ROCK1/2 and MRCK kinases, Genes Dev., 21, 562, 10.1101/gad.1484707
Sethi, 2011, Notch signalling in cancer progression and bone metastasis, Br. J. Cancer, 105, 1805, 10.1038/bjc.2011.497
Hsu, 2010, p53-Mediated transactivation of LIMK2b links actin dynamics to cell cycle checkpoint control, Oncogene, 29, 2864, 10.1038/onc.2010.40
Ebata, 2016, Functions of the tumor suppressors p53 and Rb in actin cytoskeleton remodeling, Biomed Res. Int., 2016, 1, 10.1155/2016/9231057
Croft, 2011, p53-Mediated transcriptional regulation and activation of the actin cytoskeleton regulatory RhoC to LIMK2 signaling pathway promotes cell survival, Cell Res., 21, 666, 10.1038/cr.2010.154
Yang, 2019, DIAPH1 is upregulated and inhibits cell apoptosis through ATR/p53/caspase-3 signaling pathway in laryngeal squamous cell carcinoma, Dis. Markers, 2019, 10.1155/2019/6716472
Yao, 2013, Profilin 1 potentiates apoptosis induced by staurosporine in cancer cells, Curr. Mol. Med., 13, 417
Cheng, 2013, Profilin1 sensitizes pancreatic cancer cells to irradiation by inducing apoptosis and reducing autophagy, Curr. Mol. Med., 13, 1368, 10.2174/15665240113139990060
Zaidi, 2016, Profilin potentiates chemotherapeutic agents mediated cell death via suppression of NF-κB and upregulation of p53, Apoptosis, 21, 502, 10.1007/s10495-016-1222-9
Li, 2018, A positive feedback loop of Profilin-1 and RhoA/ROCK1 promotes endothelial dysfunction and oxidative stress, Oxid. Med. Cell. Longev., 2018, 1
Belin, 2013, Visualization of actin filaments and monomers in somatic cell nuclei, Mol. Biol. Cell, 24, 982, 10.1091/mbc.e12-09-0685
Andrin, 2012, A requirement for polymerized actin in DNA double-strand break repair, Nucleus, 3, 384, 10.4161/nucl.21055
Plessner, 2019, Dynamizing nuclear actin filaments, Curr. Opin. Cell Biol., 56, 1, 10.1016/j.ceb.2018.08.005
Pfitzer, 2019, Targeting actin inhibits repair of doxorubicin-induced DNA damage: a novel therapeutic approach for combination therapy, Cell Death Dis., 10, 1, 10.1038/s41419-019-1546-9
Caridi, 2018, Nuclear F-actin and myosins drive relocalization of heterochromatic breaks, Nature, 559, 54, 10.1038/s41586-018-0242-8
Lundquist, 2014, Redox modification of nuclear actin by MICAL-2 regulates SRF signaling, Cell, 156, 563, 10.1016/j.cell.2013.12.035
Saha, 2016, G-actin guides p53 nuclear transport: potential contribution of monomeric actin in altered localization of mutant p53, Sci. Rep., 6, 32626, 10.1038/srep32626
Yan, 2012, RAC1 GTPase plays an important role in γ-irradiation induced G 2/M checkpoint activation, Breast Cancer Res., 14, 1, 10.1186/bcr3164
Huelsenbeck, 2012, Rac1 protein signaling is required for DNA damage response stimulated by topoisomerase II poisons, J. Biol. Chem., 287, 38590, 10.1074/jbc.M112.377903
Li, 2020, Rac1 activates non-oxidative pentose phosphate pathway to induce chemoresistance of breast cancer, Nat. Commun., 11
Wartlick, 2013, DNA damage response (DDR) induced by topoisomerase II poisons requires nuclear function of the small GTPase Rac, Biochim. Biophys. Acta - Mol. Cell Res., 1833, 3093, 10.1016/j.bbamcr.2013.08.016
Krauthammer, 2012, Exome sequencing identifies recurrent somatic RAC1 mutations in melanoma, Nat. Genet., 44, 1006, 10.1038/ng.2359
Deshmukh, 2017, Epidermal rac1 regulates the DNA damage response and protects from UV-light-induced keratinocyte apoptosis and skin carcinogenesis, Cell Death Dis., 8, 10.1038/cddis.2017.63
Espinha, 2015, Rac1 GTPase-deficient HeLa cells present reduced DNA repair, proliferation, and survival under UV or gamma irradiation, Mol. Cell. Biochem., 404, 281, 10.1007/s11010-015-2388-0
Hinde, 2014, Fluctuation-based imaging of nuclear Rac1 activation by protein oligomerisation, Sci. Rep., 4, 10.1038/srep04219
Hajas, 2013, 8-Oxoguanine DNA glycosylase-1 links DNA repair to cellular signaling via the activation of the small GTPase Rac1, Free Radic. Biol. Med., 61, 384, 10.1016/j.freeradbiomed.2013.04.011
Acevedo, 2018, Crosstalk between Rac1-mediated actin regulation and ROS production, Free Radic. Biol. Med., 116, 101, 10.1016/j.freeradbiomed.2018.01.008
Wilson, 2015, Regulation of cytoskeletal dynamics by redox signaling and oxidative stress: implications for neuronal development and trafficking, Front. Cell. Neurosci., 9, 381, 10.3389/fncel.2015.00381
Guo, 2003, P19Arf-p53 tumor suppressor pathway regulates cell motility by suppression of phosphoinositide 3-kinase and Rac1 GTPase activities, J. Biol. Chem., 278, 14414, 10.1074/jbc.M300341200
Yue, 2017, Gain-of-function mutant p53 activates small GTPase Rac1 through SUMOylation to promote tumor progression, Genes Dev., 31, 1641, 10.1101/gad.301564.117
Kang, 2012, DNA damage induces reactive oxygen species generation through the H2AX-Nox1/Rac1 pathway, Cell Death Dis., 3, 1, 10.1038/cddis.2011.134
Marcar, 2019, Acquired resistance of EGFR-Mutated lung cancer to tyrosine kinase inhibitor treatment promotes PARP inhibitor sensitivity, Cell Rep., 27, 3422, 10.1016/j.celrep.2019.05.058
Kogler, 2020, HACE1 prevents lung carcinogenesis via inhibition of RAC-Family GTPases, Cancer Res., 80, 3009, 10.1158/0008-5472.CAN-19-2270
Bishop, 2000, Rho GTPases and their effector proteins, Biochem. J., 348, 241, 10.1042/bj3480241
Pérez-Yépez, 2018, p21 Activated kinase 1: nuclear activity and its role during DNA damage repair, DNA Repair (Amst.), 65, 42, 10.1016/j.dnarep.2018.03.004
Singh, 2005, Nuclear localization and chromatin targets of p21-activated kinase 1, J. Biol. Chem., 280, 18130, 10.1074/jbc.M412607200
Li, 2012, MORC2 signaling integrates phosphorylation-dependent, ATPase-Coupled chromatin remodeling during the DNA damage response, Cell Rep., 2, 1657, 10.1016/j.celrep.2012.11.018
Motwani, 2013, Identification of novel gene targets and functions of p21-activated kinase 1 during dna damage by gene expression profiling, PLoS One, 8, 10.1371/journal.pone.0066585
Cruz, 2016, Reduced PAK1 activity sensitizes FA/BRCA-proficient breast cancer cells to PARP inhibition, Oncotarget, 7, 76590, 10.18632/oncotarget.12576
Qian, 2020, PAK1 silencing is synthetic lethal with CDK4/6 inhibition in gastric cancer cells via regulating PDK1 expression, Hum. Cell, 33, 377, 10.1007/s13577-019-00317-6
Gan, 2015, Dysregulation of PAK1 is associated with DNA damage and is of prognostic importance in primary esophageal small cell carcinoma, Int. J. Mol. Sci., 16, 12035, 10.3390/ijms160612035
Beesetti, 2017, Transcriptional regulation of ataxia-telangiectasia and Rad3-related protein by activated p21-activated kinase-1 protects keratinocytes in UV-B-induced premalignant skin lesions, Oncogene, 36, 6154, 10.1038/onc.2017.218
Advani, 2015, Kinase-independent role for CRAF-driving tumour radioresistance via CHK2, Nat. Commun., 6, 10.1038/ncomms9154
Roig, 2000, p21-Activated protein kinase γ-PAK is translocated and activated in response to hyperosmolarity. Implication of Cdc42 and phosphoinositide 3- kinase in a two-step mechanism for γ-PAK activation, J. Biol. Chem., 275, 16933, 10.1074/jbc.M001627200
Roig, 1999, p21-activated protein kinase γ-PAK is activated by ionizing radiation and other DNA-damaging agents. Similarities and differences to α-PAK, J. Biol. Chem., 274, 31119, 10.1074/jbc.274.44.31119
Lee, 2019, Pak2 kinase promotes cellular senescence and organismal aging, Proc. Natl. Acad. Sci. U. S. A., 116, 13311, 10.1073/pnas.1903847116
Johnson, 2013, Stimulation of in vivo nuclear transport dynamics of actin and its co-factors IQGAP1 and Rac1 in response to DNA replication stress, Biochim. Biophys. Acta - Mol. Cell Res., 1833, 2334, 10.1016/j.bbamcr.2013.06.002
Colón-Bolea, 2020, RAC1 induces nuclear alterations through the LINC complex to enhance melanoma invasiveness, Mol. Biol. Cell, 10.1091/mbc.E20-02-0127
Justilien, 2017, Ect2-dependent rRNA synthesis is required for KRAS-TRP53-Driven lung adenocarcinoma, Cancer Cell, 31, 256, 10.1016/j.ccell.2016.12.010
Liu, 2019, RNA-binding protein HuR regulates Rac1 nucleocytoplasmic shuttling through nucleophosmin in the intestinal epithelium, CMGH, 8, 475
Colomba, 2008, Activation of Rac1 and the exchange factor Vav3 are involved in NPM-ALK signaling in anaplastic large cell lymphomas, Oncogene, 27, 2728, 10.1038/sj.onc.1210921
Ascer, 2015, CDC42 gtpase activation affects hela cell DNA repair and proliferation following UV radiation-induced genotoxic stress, J. Cell. Biochem., 116, 2086, 10.1002/jcb.25166
Eduardo da Silva, 2020, Overactivated Cdc42 acts through Cdc42EP3/Borg2 and NCK to trigger DNA damage response signaling and sensitize cells to DNA-damaging agents, Exp. Cell Res., 395, 10.1016/j.yexcr.2020.112206
Farrugia, 2016, The Borg family of Cdc42 effector proteins Cdc42EP1-5, Biochem. Soc. Trans., 44, 1709, 10.1042/BST20160219
Calvo, 2015, Cdc42EP3/BORG2 and septin network enables mechano-transduction and the emergence of cancer-associated fibroblasts, Cell Rep., 13, 2699, 10.1016/j.celrep.2015.11.052
Farrugia, 2017, Cdc42 regulates Cdc42EP3 function in cancer-associated fibroblasts, Small GTPases, 8, 49, 10.1080/21541248.2016.1194952
Joo, 2005, Septins: traffic control at the cytokinesis intersection, Traffic, 6, 626, 10.1111/j.1600-0854.2005.00305.x
Bridges, 2015, Septin form and function at the cell cortex, J. Biol. Chem., 290, 17173, 10.1074/jbc.R114.634444
Kinoshita, 2006, Diversity of septin scaffolds, Curr. Opin. Cell Biol., 18, 54, 10.1016/j.ceb.2005.12.005
Kremer, 2007, Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7, Cell, 130, 837, 10.1016/j.cell.2007.06.053
Errington, 2013, Depletion of the adaptor protein NCK increases UV-Induced p53 phosphorylation and promotes apoptosis, PLoS One, 8, 10.1371/journal.pone.0076204
Vanni, 2005, Constitutively active Cdc42 mutant confers growth disadvantage in cell transformation, Cell Cycle, 4, 1675, 10.4161/cc.4.11.2170
Wang, 2005, Cdc42GAP regulates c-Jun N-terminal kinase (JNK)-mediated apoptosis and cell number during mammalian perinatal growth, Proc. Natl. Acad. Sci. U. S. A., 102, 13484, 10.1073/pnas.0504420102
Sluss, 2006, H2AX is a target of the JNK signaling pathway that is required for apoptotic DNA fragmentation, Mol. Cell, 23, 152, 10.1016/j.molcel.2006.07.001
Jaffer, 2002, p21-Activated kinases: three more join the Pak, Int. J. Biochem. Cell Biol., 34, 713, 10.1016/S1357-2725(01)00158-3
Wells, 2010, The emerging importance of group II PAKs, Biochem. J., 425, 465, 10.1042/BJ20091173
Abo, 1998
Cammarano, 2005, Pak4 induces premature senescence via a pathway requiring p16INK4/p19ARF and mitogen-activated protein kinase signaling, Mol. Cell. Biol., 25, 9532, 10.1128/MCB.25.21.9532-9542.2005
Callow, 2002, Requirement for PAK4 in the anchorage-independent growth of human cancer cell lines, J. Biol. Chem., 277, 550, 10.1074/jbc.M105732200
Silva, 2019, Proteomic and interactome approaches reveal PAK4, PHB-2, and 14-3-3ν as targets of overactivated cdc42 in cellular responses to genomic instability, J. Proteome Res., 18, 3597, 10.1021/acs.jproteome.9b00260
Li, 2019, Dual PAK4-NAMPT inhibition impacts growth and survival, and increases sensitivity to DNA-damaging agents in Waldenstrom Є macroglobulinemia, Clin. Cancer Res., 25, 369, 10.1158/1078-0432.CCR-18-1776
Li, 2012, Nucleo-cytoplasmic shuttling of PAK4 modulates β-catenin intracellular translocation and signaling, Biochim. Biophys. Acta - Mol. Cell Res., 1823, 465, 10.1016/j.bbamcr.2011.11.013
Karimaian, 2017, The crosstalk between Wnt/β-catenin signaling pathway with DNA damage response and oxidative stress: implications in cancer therapy, DNA Repair (Amst.), 51, 14, 10.1016/j.dnarep.2017.01.003
Zhao, 2018, The role of canonical wnt signaling in regulating radioresistance, Cell. Physiol. Biochem., 48, 419, 10.1159/000491774
Serebryannyy, 2017, Nuclear α-catenin mediates the DNA damage response via β-catenin and nuclear actin, J. Cell. Sci., 130, 1717
Dan, 2002, PAK5, a new brain-specific kinase, promotes neurite outgrowth in N1E-115 cells, Mol. Cell. Biol., 22, 567, 10.1128/MCB.22.2.567-577.2002
Cau, 2001, A novel p21-activated kinase binds the actin and microtubule networks and induces microtubule stabilization, J. Cell Biol., 155, 1029, 10.1083/jcb.200104123
Cotteret, 2003, p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD, Mol. Cell. Biol., 23, 5526, 10.1128/MCB.23.16.5526-5539.2003
Zhang, 2015, p21-Activated kinase 5 affects cisplatin-induced apoptosis and proliferation in hepatocellular carcinoma cells, Tumor Biol., 36, 3685, 10.1007/s13277-014-3007-5
Baskaran, 2012, Group I and II mammalian PAKs have different modes of activation by Cdc42, EMBO Rep., 13, 653, 10.1038/embor.2012.75
Selamat, 2015, The Cdc42 effector kinase PAK4 localizes to cell-cell junctions and contributes to establishing cell polarity, PLoS One, 10, 10.1371/journal.pone.0129634
Morse, 2016, PAK6 targets to cell-cell adhesions through its N-terminus in a Cdc42-dependent manner to drive epithelial colony escape, J. Cell. Sci., 129, 380
Carlier, 1999, Signalling to actin: the Cdc42-N-WASP-Arp2/3 connection, Chem. Biol., 6, 10.1016/S1074-5521(99)80107-0
Rohatgi, 1999, The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly, Cell, 97, 221, 10.1016/S0092-8674(00)80732-1
Rohatgi, 2000, Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4,5-bisphosphate, J. Cell Biol., 150, 1299, 10.1083/jcb.150.6.1299
Suetsugu, 2003, Translocation of N-WASP by nuclear localization and export signals into the nucleus modulates expression of HSP90, J. Biol. Chem., 278, 42515, 10.1074/jbc.M302177200
Looi, 2014, The open conformation of WASP regulates its nuclear localization and gene transcription in myeloid cells, Int. Immunol., 26, 341, 10.1093/intimm/dxt072
Schrank, 2018, Nuclear ARP2/3 drives DNA break clustering for homology-directed repair, Nature, 559, 61, 10.1038/s41586-018-0237-5
Sadhukhan, 2014, Nuclear role of WASp in gene transcription is uncoupled from its ARP2/3-Dependent cytoplasmic role in actin polymerization, J. Immunol., 193, 150, 10.4049/jimmunol.1302923
Williams, 2003, The polybasic region of Ras and Rho family small GTPases: a regulator of protein interactions and membrane association and a site of nuclear localization signal sequences, Cell. Signal., 15, 1071, 10.1016/S0898-6568(03)00098-6
