Rho GTPases in neurodegeneration diseases
Abstract
Rho GTPases are molecular switches that modulate multiple intracellular signaling processes by means of various effector proteins. As a result, Rho GTPase activities are tightly spatiotemporally regulated in order to ensure homeostasis within the cell. Though the roles of Rho GTPases during neural development have been well documented, their participation during neurodegeneration has been far less characterized. Herein we discuss our current knowledge of the role and function of Rho GTPases and regulators during neurodegeneration, and highlight their potential as targets for therapeutic intervention in common neurodegenerative disorders.
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In mammals, the RHO family consists of 20 members distributed into eight subfamilies based on sequence homology.
“In mammals, the RHO family consists of 20 members in total, further distributed into eight subfamilies based on sequence homology: CDC42, RAC, RHO, RHOBTB, RHOD/F, RHOH, RHOU/V, and RND (9).”
From RHO to the DOCK for GDP disembarking: Structural insights into the DOCK GTPase nucleotide exchange factors (2021) · cites this paper as [9]
Dysregulation of Rho GTPases has been studied in relation to cancer progression, but accumulating evidence supports a role in traumatic brain injury and neurodegenerative diseases.
“Dysregulation of Rho GTPases has been studied in relation to cancer progression for a number of years [3], but accumulating evidence supports a role in traumatic brain injury and neurodegenerative diseases as well [4,5,6,7].”
From RhoA Signaling in Neurodegenerative Diseases (2022) · cites this paper as [4]
Emerging evidence points toward a role of aberrant RhoA signaling in neurodegenerative diseases such as Parkinson's disease, Alzheimer's disease, Huntington's disease, and amyotrophic lateral sclerosis.
“Indeed, emerging evidence points toward a role of aberrant RhoA signaling in neurodegenerative diseases such as Parkinson’s disease, Alzheimer’s disease, Huntington’s disease, and amyotrophic lateral sclerosis.”
From RhoA Signaling in Neurodegenerative Diseases (2022) · cites this paper as [4]
Cites
Rosen, D. R., Siddique, T., Patterson, D., Figlewicz, D. A., Sapp, P., Hentati, A., Donaldson, D., Goto, J., O'Regan, J. P., Deng, H.-X., et al. (1993) · Nature · doi:10.1038/362059a0 · Cited by 7,062 · see citing works
Ridley, A. J., & Hall, A. (1992) · Cell · doi:10.1016/0092-8674(92)90163-7 · Cited by 4,469 · see citing works
Nobes, C. D., & Hall, A. (1995) · Cell · doi:10.1016/0092-8674(95)90370-4 · Cited by 4,414 · see citing works
The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D., & Hall, A. (1992) · Cell · doi:10.1016/0092-8674(92)90164-8 · Cited by 3,651 · see citing works
RHO GTPASES: Biochemistry and Biology
Jaffe, A. B., & Hall, A. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.020604.150721 · Cited by 3,009 · see citing works
Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)
Kimura, K., Ito, M., Amano, M., Chihara, K., Fukata, Y., Nakafuku, M., Yamamori, B., Feng, J., Nakano, T., Okawa, K., et al. (1996) · Science · doi:10.1126/science.273.5272.245 · Cited by 2,889 · see citing works
Molecular Pathways of Neurodegeneration in Parkinson's Disease
Dawson, T. M., & Dawson, V. L. (2003) · Science · doi:10.1126/science.1087753 · Cited by 1,659 · see citing works
Signaling from Rho to the Actin Cytoskeleton Through Protein Kinases ROCK and LIM-kinase
Maekawa, M., Ishizaki, T., Boku, S., Watanabe, N., Fujita, A., Iwamatsu, A., Obinata, T., Ohashi, K., Mizuno, K., & Narumiya, S. (1999) · Science · doi:10.1126/science.285.5429.895 · Cited by 1,640 · see citing works
UNRAVELING THE MECHANISMS INVOLVED IN MOTOR NEURON DEGENERATION IN ALS
Bruijn, L. I., Miller, T. M., & Cleveland, D. W. (2004) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.27.070203.144244 · Cited by 1,371 · see citing works
Rohatgi, R., Ma, L., Miki, H., Lopez, M., Kirchhausen, T. L., Takenawa, T., & Kirschner, M. W. (1999) · Cell · doi:10.1016/s0092-8674(00)80732-1 · Cited by 1,350 · see citing works
Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
Yang, N., Higuchi, O., Ohashi, K., Nagata, K., Wada, A., Kangawa, K., Nishida, E., & Mizuno, K. (1998) · Nature · doi:10.1038/31735 · Cited by 1,296 · see citing works
Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
Edwards, D. C., Sanders, L. C., Bokoch, G., & Gill, G. N. (1999) · Nature Cell Biology · doi:10.1038/12963 · Cited by 1,065 · see citing works
The role of the Rho GTPases in neuronal developmentPreprint
Govek, E., Newey, S. E., & Aelst, L. V. (2005) · Genes & Development · doi:10.1101/gad.1256405 · Cited by 986 · see citing works
Neuropathological assessment of Parkinson’s disease: refining the diagnostic criteria
Dickson, D. W., Braak, H., Duda, J. E., Duyckaerts, C., Gasser, T., Halliday, G. M., Hardy, J., Leverenz, J. B., Del Tredici, K., Wszolek, Z. K., et al. (2009) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70238-8 · Cited by 972 · see citing works
Genetic and clinical aspects of Charcot‐Marie‐Tooth's disease
Skre, H. (1974) · Clinical Genetics · doi:10.1111/j.1399-0004.1974.tb00638.x · Cited by 917 · see citing works
p75 interacts with the Nogo receptor as a co-receptor for Nogo, MAG and OMgp
Wang, K., Kim, J. A., Sivasankaran, R., Segal, R. A., & He, Z. (2002) · Nature · doi:10.1038/nature01176 · Cited by 819 · see citing works
A cAMP-response element binding protein-induced microRNA regulates neuronal morphogenesis
Vo, N., Klein, M. E., Varlamova, O., Keller, D. M., Yamamoto, T. S., Goodman, R. H., & Impey, S. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508448102 · Cited by 799 · see citing works
The trip of the tip: understanding the growth cone machinery
Lowery, L. A., & Vactor, D. V. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2679 · Cited by 794 · see citing works
Gervais, F. G., Xu, D., Robertson, G. S., Vaillancourt, J. P., Zhu, Y., Huang, J., LeBlanc, A. C., Smith, D., Rigby, M., Shearman, M. S., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80748-5 · Cited by 784 · see citing works
Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex
Machesky, L. M., Mullins, R. D., Higgs, H. N., Kaiser, D. A., Blanchoin, L., May, R. C., Hall, M. E., & Pollard, T. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3739 · Cited by 773 · see citing works
Zhang, S., Han, J., Sells, M. A., Chernoff, J., Knaus, U. G., Ulevitch, R. J., & Bokoch, G. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.23934 · Cited by 726 · see citing works
A century-old debate on protein aggregation and neurodegeneration enters the clinic
Lansbury, P. T., & Lashuel, H. A. (2006) · Nature · doi:10.1038/nature05290 · Cited by 681 · see citing works
Rho Kinase Inhibition Enhances Axonal Regeneration in the Injured CNS
Fournier, A. E., Takizawa, B. T., & Strittmatter, S. M. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-04-01416.2003 · Cited by 644 · see citing works
Bagrodia, S., Dérijard, B., Davis, R. J., & Cerione, R. A. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.27995 · Cited by 635 · see citing works
Activation of the nuclear factor-kappaB by Rho, CDC42, and Rac-1 proteins.Preprint
Perona, R., Montaner, S., Saniger, L., Sánchez‐Pérez, I., Bravo, R., & Lacal, J. C. (1997) · Genes & Development · doi:10.1101/gad.11.4.463 · Cited by 608 · see citing works
Inhibition of Myosin Light Chain Kinase by p21-Activated Kinase
Sanders, L. C., Matsumura, F., Bokoch, G., & de Lanerolle, P. (1999) · Science · doi:10.1126/science.283.5410.2083 · Cited by 593 · see citing works
mDia mediates Rho-regulated formation and orientation of stable microtubules
Palazzo, A. F., Cook, T. A., Alberts, A. S., & Gundersen, G. G. (2001) · Nature Cell Biology · doi:10.1038/35087035 · Cited by 582 · see citing works
Rowland, L. P. (1993) · Mayo Clinic Proceedings · doi:10.1016/s0025-6196(12)62285-x · Cited by 581 · see citing works
Lamarche, N., Tapon, N., Stowers, L., Burbelo, P. D., Aspenström, P., Bridges, T., Chant, J., & Hall, A. (1996) · Cell · doi:10.1016/s0092-8674(00)81371-9 · Cited by 572 · see citing works
Signal Transduction in Neuronal Migration
Wong, K., Ren, X.-R., Huang, Y.-Z., Xie, Y., Liu, G., Saito, H., Tang, H., Wen, L., Brady‐Kalnay, S. M., Mei, L., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00530-x · Cited by 550 · see citing works
Ohashi, K., Nagata, K., Maekawa, M., Ishizaki, T., Narumiya, S., & Mizuno, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.5.3577 · Cited by 533 · see citing works
PirB is a Functional Receptor for Myelin Inhibitors of Axonal Regeneration
Atwal, J. K., Pinkston-Gosse, J., Syken, J., Stawicki, S. S., Wu, Y., Shatz, C. J., & Tessier‐Lavigne, M. (2008) · Science · doi:10.1126/science.1161151 · Cited by 503 · see citing works
Rho Guanine Dissociation Inhibitors
Olofsson, B. (1999) · Cellular Signalling · doi:10.1016/s0898-6568(98)00063-1 · Cited by 491 · see citing works
Current knowledge of the large RhoGAP family of proteins
Tcherkezian, J., & Lamarche‐Vane, N. (2007) · Biology of the Cell · doi:10.1042/bc20060086 · Cited by 475 · see citing works
Self-citationThe p75 receptor acts as a displacement factor that releases Rho from Rho-GDI
Yamashita, T., & Tohyama, M. (2003) · Nature Neuroscience · doi:10.1038/nn1045 · Cited by 460 · see citing works
Aggresomes Formed by α-Synuclein and Synphilin-1 Are Cytoprotective
Tanaka, M., Kim, Y. M., Lee, G., Junn, E., Iwatsubo, T., & Mouradian, M. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310994200 · Cited by 421 · see citing works
Post-translational modifications of p21rho proteins.
Adamson, P., Marshall, C. J., Hall, A., & Tilbrook, P. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)88661-1 · Cited by 421 · see citing works
Niederöst, B. P., Oertle, T., Fritsche, J., McKinney, R. A., & Bandtlow, C. E. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-23-10368.2002 · Cited by 415 · see citing works
Dbl family guanine nucleotide exchange factors
Zheng, Y. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(01)01973-9 · Cited by 413 · see citing works
Disrupted-in-Schizophrenia 1 (DISC1) regulates spines of the glutamate synapse via Rac1
Hayashi-Takagi, A., Takaki, M., Graziane, N., Seshadri, S., Murdoch, H., Dunlop, A. J., Makino, Y., Seshadri, A. J., Ishizuka, K., Srivastava, D. P., et al. (2010) · Nature Neuroscience · doi:10.1038/nn.2487 · Cited by 399 · see citing works
Ubiquitin, cellular inclusions and their role in neurodegeneration
Alves-Rodrigues, A., Gregori, L., & Figueiredo-Pereira, M. E. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01276-4 · Cited by 393 · see citing works
Park, J. B., Yiu, G. C., Kaneko, S., Wang, J., Chang, J., & He, Z. (2005) · Neuron · doi:10.1016/j.neuron.2004.12.040 · Cited by 388 · see citing works
A microRNA-based gene dysregulation pathway in Huntington's disease
Johnson, R., Zuccato, C., Belyaev, N. D., Guest, D. J., Cattaneo, E. F., & Buckley, N. J. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.11.001 · Cited by 360 · see citing works
Hereditary motor and sensory neuropathies.
Vance, J. M. (1991) · Journal of Medical Genetics · doi:10.1136/jmg.28.1.1 · Cited by 348 · see citing works
RhoE Binds to ROCK I and Inhibits Downstream Signaling
Riento, K., Guasch, R., Garg, R., Jin, B.-Q., & Ridley, A. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.12.4219-4229.2003 · Cited by 324 · see citing works
Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease
Zhao, L., Ma, Q.-L., Calon, F., Harris-White, M. E., Yang, F., Lim, G. P., Morihara, T., Ubeda, O. J., Ambegaokar, S., Hansen, J. E., et al. (2006) · Nature Neuroscience · doi:10.1038/nn1630 · Cited by 317 · see citing works
Nonsteroidal Anti-Inflammatory Drugs Can Lower Amyloidogenic Aß <sub>42</sub> by Inhibiting Rho
Zhou, Y., Su, Y., Li, B., Liu, F., Ryder, J. W., Wu, X., Gonzalez-DeWhitt, P. A., Gelfanova, V., Hale, J. E., May, P. C., et al. (2003) · Science · doi:10.1126/science.1090154 · Cited by 316 · see citing works
VAV proteins as signal integrators for multi-subunit immune-recognition receptors
Turner, M., & Billadeau, D. D. (2002) · Nature reviews. Immunology · doi:10.1038/nri840 · Cited by 312 · see citing works
Alzheimer-like neurodegeneration in aged antinerve growth factor transgenic mice
Capsoni, S., Ugolini, G., Comparini, A., Ruberti, F., Berardi, N., & Cattaneo, A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.12.6826 · Cited by 279 · see citing works
Otomo, A. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg184 · Cited by 250 · see citing works
Rnd Proteins Function as RhoA Antagonists by Activating p190 RhoGAP
Wennerberg, K., Forget, M.-A., Ellerbroek, S. M., Arthur, W. T., Burridge, K., Settleman, J. E., Der, C. J., & Hansen, S. H. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00418-4 · Cited by 247 · see citing works
Developmental axon pruning mediated by BDNF-p75NTR–dependent axon degeneration
Singh, K. K., Park, K. J., Hong, E. J., Kramer, B. M., Greenberg, M. E., Kaplan, D. R., & Miller, F. D. (2008) · Nature Neuroscience · doi:10.1038/nn.2114 · Cited by 237 · see citing works
Côté, J., Motoyama, A. B., Bush, J., & Vuori, K. (2005) · Nature Cell Biology · doi:10.1038/ncb1280 · Cited by 222 · see citing works
Eblen, S. T., Slack, J. K., Weber, M. J., & Catling, A. D. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.17.6023-6033.2002 · Cited by 222 · see citing works
Suppression of Rho-kinase activity promotes axonal growth on inhibitory CNS substrates
Borisoff, J., Chan, C. C. M., Hiebert, G. W., Oschipok, L. W., Robertson, G. S., Zamboni, R. J., Steeves, J. D., & Tetzlaff, W. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/s1044-7431(02)00032-5 · Cited by 210 · see citing works
Li, X., Saint-Cyr-Proulx, E., Aktories, K., & Lamarche‐Vane, N. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109913200 · Cited by 199 · see citing works
Self-citationPetratos, S., Li, Q.-X., George, A. J., Hou, X., Kerr, M. L., Unabia, S. E., Hatzinisiriou, I., Maksel, D., Aguilar, M.-I., & Small, D. H. (2008) · Brain · doi:10.1093/brain/awm260 · Cited by 197 · see citing works
WASP and SCAR/WAVE proteins: the drivers of actin assembly
Pollitt, A. Y., & Insall, R. H. (2009) · Journal of Cell Science · doi:10.1242/jcs.023879 · Cited by 184 · see citing works
Cdc42-interacting Protein 4 Mediates Binding of the Wiskott-Aldrich Syndrome Protein to Microtubules
Tian, L., Nelson, D. L., & Stewart, D. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.11.7854 · Cited by 180 · see citing works
Hereditary Motor and Sensory Neuropathies
Schröder, J. M. (2001) · Springer eBooks · doi:10.1007/978-3-642-56808-4_7 · Cited by 174 · see citing works
Phosphorylation of profilin by ROCK1 regulates polyglutamine aggregation
Shao, J., Welch, W. J., DiProspero, N. A., & Diamond, M. I. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00079-08 · Cited by 171 · see citing works
Identification of Epigenetically Altered Genes in Sporadic Amyotrophic Lateral Sclerosis
Figueroa‐Romero, C., Hur, J., Bender, D. E., Delaney, C. E., Cataldo, M. D., Smith, A. L., Yung, R. L., Ruden, D. M., Callaghan, B. C., & Feldman, E. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0052672 · Cited by 161 · see citing works
A rapid cellular FRET assay of polyglutamine aggregation identifies a novel inhibitor
Pollitt, S. K., Pallos, J., Shao, J., Desai, U. A., Ma, A. A. K., Thompson, L. M., Marsh, J. L., & Diamond, M. I. (2003) · Neuron · doi:10.1016/s0896-6273(03)00697-4 · Cited by 151 · see citing works
Barcia, C., Ros, C. M., Annese, V., Carrillo-de Sauvage, M. A., Ros-Bernal, F., Gómez, A., Yuste, J. E., Campuzano, C. M., de Pablos, V., Fernandez-Villalba, E., et al. (2012) · Scientific Reports · doi:10.1038/srep00809 · Cited by 150 · see citing works
Stendel, C., Roos, A., Deconinck, T., Pereira, J. A., Castagner, F., Niemann, A., Kirschner, J., Korinthenberg, R., Ketelsen, U., Battaloğlu, E., et al. (2007) · American Journal of Human Genetics · doi:10.1086/518770 · Cited by 140 · see citing works
Colomer, V. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.9.1519 · Cited by 127 · see citing works
A Role for Nogo Receptor in Macrophage Clearance from Injured Peripheral Nerve
Fry, E. J., Ho, C., & David, S. (2007) · Neuron · doi:10.1016/j.neuron.2007.02.009 · Cited by 126 · see citing works
Hereditary Motor and Sensory Neuropathy
(2013) · Springer eBooks · doi:10.1007/978-3-642-28753-4_200929 · Cited by 123 · see citing works
Rac1 Protein Rescues Neurite Retraction Caused by G2019S Leucine-rich Repeat Kinase 2 (LRRK2)
Chan, D., Citro, A., Cordy, J. M., Shen, G. C., & Wolozin, B. L. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.234005 · Cited by 120 · see citing works
Verhoeven, K., Jonghe, P. D., de Putte, T. V., Nelis, E., Zwijsen, A., Verpoorten, N., Vriendt, E. D., Jacobs, A., Gerwen, V. V., Francis, A., et al. (2003) · The American Journal of Human Genetics · doi:10.1086/378159 · Cited by 118 · see citing works
Nitric Oxide as an Initiator of Brain Lesions During the Development of Alzheimer Disease
Aliev, G. M., Palacios, H. H., Lipsitt, A. E., Fischbach, K., Lamb, B. T., Obrenovich, M. E., Morales, L., Gasimov, E. K., & Bragin, V. (2009) · Neurotoxicity Research · doi:10.1007/s12640-009-9066-5 · Cited by 112 · see citing works
Park, K. J., Ayala‐Grosso, C. A., Aubert, I., Kaplan, D. R., & Miller, F. D. (2010) · Nature Neuroscience · doi:10.1038/nn.2513 · Cited by 111 · see citing works
Aβ1-42 stimulates actin polymerization in hippocampal neurons through Rac1 and Cdc42 Rho GTPases
Mendoza‐Naranjo, A., González-Billault, C. E., & Maccioni, R. B. (2007) · Journal of Cell Science · doi:10.1242/jcs.03323 · Cited by 107 · see citing works
Actin Polymerization Is Essential for Myelin Sheath Fragmentation during Wallerian Degeneration
Jung, J., Cai, W., Lee, H. K., Pellegatta, M., Shin, Y. K., Jang, S. Y., Suh, D. J., Wrabetz, L. G., Feltri, M. L., & Park, H. T. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.4537-10.2011 · Cited by 106 · see citing works
Kanekura, K., Hashimoto, Y., Kita, Y. A., Sasabe, J., Aiso, S., Nishimoto, I., & Matsuoka, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410508200 · Cited by 99 · see citing works
Maystadt, I., Rezsöhazy, R., Barkats, M., Duqué, S. I., Vannuffel, P., Remacle, S., Lambert, B., Najimi, M., Sokal, E. M., Münnich, A., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/518900 · Cited by 92 · see citing works
Peng, Y., He, W., Tang, J. Y., Tao, T., Chen, C., Gao, Y., Zhang, W., He, X., Dai, Y., Zhu, N.-C., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.096537 · Cited by 92 · see citing works
Transgenic mice overexpressing XIAP in neurons show better outcome after transient cerebral ischemia
Trapp, T., Korhonen, L., Besselmann, M., Maza, R. M., MERCER, E. A. J., & Lindholm, D. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/s1044-7431(03)00013-7 · Cited by 89 · see citing works
ALS2/Alsin Regulates Rac-PAK Signaling and Neurite Outgrowth
Tudor, E. L., Perkinton, M. S., Schmidt, A., Ackerley, S., Brownlees, J., Jacobsen, J. O. N., Byers, H. L., Ward, M. A., Hall, A., Leigh, P. N., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506216200 · Cited by 85 · see citing works
Dock3 induces axonal outgrowth by stimulating membrane recruitment of the WAVE complex
Namekata, K., Harada, C., Taya, C., Guo, X., Kimura, H., Parada, L. F., & Harada, T. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914514107 · Cited by 84 · see citing works
Yamanaka, K., Velde, C. V., Eymard-Pierre, É., Bertini, E., Boespflug‐Tanguy, O., & Cleveland, D. W. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2635267100 · Cited by 84 · see citing works
Altered distribution of RhoA in Alzheimer’s disease and AβPP overexpressing mice
Huesa, G., Baltrons, M. A., Gómez-Ramos, P., Morán, A., García, A., Hidalgo, J., Francés, S., Santpere, G., Ferrer, I., & Galea, E. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-1203 · Cited by 82 · see citing works
Holbert, S., Dedeoglu, A., Humbert, S., Saudou, F., Ferrante, R. J., & Néri, C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0437967100 · Cited by 79 · see citing works
Dock3 Stimulates Axonal Outgrowth via GSK-3β-Mediated Microtubule Assembly
Namekata, K., Harada, C., Guo, X., Kimura, A. K., Kittaka, D., Watanabe, H., & Harada, T. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.4884-11.2012 · Cited by 79 · see citing works
Progressive spinal axonal degeneration and slowness in ALS2‐deficient mice
Yamanaka, K., Miller, T. M., McAlonis‐Downes, M., Chun, S. J., & Cleveland, D. W. (2006) · Annals of Neurology · doi:10.1002/ana.20888 · Cited by 77 · see citing works
Isolation and Characterization of Novel Presenilin Binding Protein
Kashiwa, A., Yoshida, H., Lee, S., Paladino, T., Liu, Y., Chen, Q., Dargusch, R., Schubert, D. A., & Kimura, H. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750109.x · Cited by 69 · see citing works
Horn, M., Baumann, R., Pereira, J. A., Sidiropoulos, P. N. M., Somandin, C., Welzl, H., Stendel, C., Lühmann, T., Wessig, C., Toyka, K., et al. (2012) · Brain : a journal of neurology · doi:10.1093/brain/aws275 · Cited by 67 · see citing works
Vega, F. M. D. L., & Ridley, A. J. (2007) · Cell · doi:10.1016/j.cell.2007.06.021 · Cited by 67 · see citing works
VAV2 and VAV3 as Candidate Disease Genes for Spontaneous Glaucoma in Mice and Humans
Fujikawa, K., Iwata, T., Inoue, K., Akahori, M., Kadotani, H., Fukaya, M., Watanabe, M., Chang, Q., Barnett, E. M., & Swat, W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009050 · Cited by 67 · see citing works
Loss of Modifier of Cell Adhesion Reveals a Pathway Leading to Axonal Degeneration
Chen, Q., Peto, C. A., Shelton, G. D., Mizisin, A. P., Sawchenko, P. E., & Schubert, D. A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3985-08.2009 · Cited by 65 · see citing works
Kalirin, a Key Player in Synapse Formation, Is Implicated in Human Diseases
Mandela, P., & Ma, X. (2012) · Neural Plasticity · doi:10.1155/2012/728161 · Cited by 63 · see citing works
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Chen, Q., Kimura, H., & Schubert, D. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200110151 · Cited by 63 · see citing works
Ross, C. A. (2004) · Cell · doi:10.1016/j.cell.2004.06.022 · Cited by 61 · see citing works
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Schulz, A., Baader, S. L., Niwa‐Kawakita, M., Jung, M. J., Bauer, R., Garcia, C. M., Zoch, A., Schacke, S., Hagel, C., Mautner, V., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3348 · Cited by 57 · see citing works
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Brabeck, C., Beschorner, R., Conrad, S., Mittelbronn, M. G. A., Bekure, K., Meyermann, R., Schluesener, H. J., & Schwab, J. M. (2004) · Journal of Neurotrauma · doi:10.1089/0897715041269597 · Cited by 57 · see citing works
Youn, H., Ji, I., Ji, H. P., Markesbery, W. R., & Ji, T. H. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-12309 · Cited by 56 · see citing works
Rosário, M., Schuster, S., Jüttner, R., Parthasarathy, S., Tarabykin, V. S., & Birchmeier, W. (2012) · Genes & Development · doi:10.1101/gad.191593.112 · Cited by 53 · see citing works
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Bai, N., Hayashi, H., Aida, T., Namekata, K., Harada, T., Mishina, M., & Tanaka, K. (2013) · Molecular Brain · doi:10.1186/1756-6606-6-22 · Cited by 49 · see citing works
Mocholí, E., Ballester‐Lurbe, B., Arqué, G., Poch, E., Peris, B., Guerri, C., Dierssen, M., Guasch, R. M., Terrado, J., & Pérez‐Roger, I. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019236 · Cited by 45 · see citing works
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Wang, S., Xu, B., Liou, L.-C., Ren, Q., Huang, S., Luo, Y., Zhang, Z., & Witt, S. N. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206286109 · Cited by 43 · see citing works
Mohamed, A., Saavedra, L., Pardo, A. D., Sipione, S., & Chaves, E. (2012) · Journal of Neuroscience · doi:10.1523/jneurosci.0630-12.2012 · Cited by 41 · see citing works
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Barger, S. W., Moerman-Herzog, A. M., & Mao, X. R. (2005) · Current Pharmaceutical Design · doi:10.2174/1381612053381594 · Cited by 39 · see citing works
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Oliver, A. W., He, X. T., Borthwick, K. J., Donne, A. J., Hampson, L., & HAMPSON, I. N. (2010) · British Journal of Cancer · doi:10.1038/sj.bjc.6606026 · Cited by 39 · see citing works
Rosário, M., Franke, R., Bednarski, C., & Birchmeier, W. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200609146 · Cited by 37 · see citing works
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Harrington, A., Li, Q. M., Tep, C., Park, J. B., He, Z., & Yoon, S. O. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802188200 · Cited by 37 · see citing works
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Chen, Q., Yoshida, H., Schubert, D., Maher, P. A., Mallory, M. E., & Masliah, E. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63005-2 · Cited by 33 · see citing works
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Self-citationNeuronal polarization is impaired in mice lacking RhoE expression
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Varma, H., Yamamoto, A., Sarantos, M. R., Hughes, R. E., & Stockwell, B. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.125542 · Cited by 26 · see citing works
Increased RhoA Prenylation in the loechrig (loe) Mutant Leads to Progressive Neurodegeneration
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Taléns‐Visconti, R., Peris, B., Guerri, C., & Guasch, R. M. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06526.x · Cited by 22 · see citing works
Involvement of EphB/Ephrin-B Signaling in Axonal Survival in Mouse Experimental Glaucoma
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A novel Rac1 GAP splice variant relays poly-Ub accumulation signals to mediate Rac1 inactivation
Huang, T. Y., Michael, S. A., Xu, T., Sarkeshik, A., Moresco, J. J., Yates, J. R., Masliah, E., Bokoch, G., & DerMardirossian, C. M. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e12-07-0565 · Cited by 19 · see citing works
Kamasani, U. R., & Prendergast, G. C. (2005) · Cancer Biology & Therapy · doi:10.4161/cbt.4.3.1498 · Cited by 16 · see citing works
Blanke, S., & Jäckle, H. (2006) · The FASEB Journal · doi:10.1096/fj.05-5376com · Cited by 16 · see citing works
Altered apoptotic responses in neurons lacking RhoB GTPase
Barberan-Martin, S., McNair, K., Iqbal, K., Smith, N. C., Prendergast, G. C., Stone, T. W., Cobb, S., & MORRIS, B. J. (2011) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2011.07891.x · Cited by 15 · see citing works
Tsai, Y.-C., Rieß, O., Soehn, A. S., & Nguyen, H. P. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051999 · Cited by 14 · see citing works
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Civiero, L., Cirnaru, M., Beilina, A. G., Rodella, U., Russo, I., Belluzzi, E., Lobbestael, E., Reyniers, L., Hondhamuni, G., Lewis, P. A., et al. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13369 · Cited by 66 · see citing works
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“In mammals, the RHO family consists of 20 members in total, further distributed into eight subfamilies based on sequence homology: CDC42, RAC, RHO, RHOBTB, RHOD/F, RHOH, RHOU/V, and RND (9).”
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Rayner, M., Kellaway, S. C., Kingston, I., Guillemot‐Legris, O., Gregory, H. N., Healy, J., & Phillips, J. B. (2022) · Cells · doi:10.3390/cells12010042 · Cited by 5 · see citing works
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da Silva, M. I. O., Lopes, C. S., & Liz, M. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-70377-4 · Cited by 4 · see citing works
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Ushakumary, M. G., Sontag, R. L., Posso, C., Fillmore, T., Topping, M. E., Olson, H. M., Jager, P. L. D., Bennett, D. A. A., Arvanitakis, Z., & Petyuk, V. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02573-6 · Cited by 3 · see citing works
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Zhang, H. (2016) · Infection International/Infection International (Electronic Edition) · doi:10.1515/ii-2017-0134
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Dipol, T., Morsilli, O., Fortuna, A., Zecca, V., Palombelli, G., Maroccia, Z., Belfiore, M., Campana, G., Ricceri, L., Feligioni, M., et al. (2026) · Pharmacological Reports · doi:10.1007/s43440-026-00838-6
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- Authors
- DeGeer, J., & Lamarche-Vane, N.
- Affiliations
- McGill University (CA)
- ORCID
- DeGeer, Jonathan
- Venue
- Experimental Cell Research
- Publisher
- Elsevier BV
- Published
- 2013-09
- Volume
- 319
- Issue
- 15
- Pages
- 2384-2394
- ISSN
- 0014-4827 (ISSN-L)
- OpenAlex
- W1976841911
- Cited by
- 46
- References
- 119
- Citations by year
- 2026: 4 · 2025: 3 · 2024: 2 · 2023: 3 · 2022: 2 · 2021: 8 · 2020: 5 · 2019: 3 · 2018: 1 · 2017: 2 · 2016: 3 · 2015: 7 · 2014: 3
- FWCI
- 0.41
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Experimental Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Canadian Institutes of Health Research (MOP-14701)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- Rho GTPases, neurodegeneration, intracellular signaling, effector proteins, therapeutic target, neurodegenerative diseases
- MeSH terms
- Animals, Gene Expression Regulation, Humans, Isoenzymes, Nerve Regeneration, Signal Transduction, Neurites, Neurodegenerative Diseases, Optic Nerve Injuries, rho GTP-Binding Proteins, Mice, Neurogenesis, Peripheral Nerve Injuries
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