RhoA as a Key Regulator of Innate and Adaptive Immunity

Bros, Matthias; Haas, Katharina; Moll, Lorna; Grabbe, Stephan

doi:10.3390/cells8070733

Cited by 193Protein Kinase Regulation and GTPase SignalingImmune Response and InflammationChemokine receptors and signaling

RhoA as a Key Regulator of Innate and Adaptive Immunity

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Bros, Matthias, Haas, Katharina, Moll, Lorna, Grabbe, Stephan·2019·Cells

DOI 10.3390/cells8070733PMC PMC6678964

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Abstract

RhoA is a ubiquitously expressed cytoplasmic protein that belongs to the family of small GTPases. RhoA acts as a molecular switch that is activated in response to binding of chemokines, cytokines, and growth factors, and via mDia and the ROCK signaling cascade regulates the activation of cytoskeletal proteins, and other factors. This review aims to summarize our current knowledge on the role of RhoA as a general key regulator of immune cell differentiation and function. The contribution of RhoA for the primary functions of innate immune cell types, namely neutrophils, macrophages, and conventional dendritic cells (DC) to (i) get activated by pathogen-derived and endogenous danger signals, (ii) migrate to sites of infection and inflammation, and (iii) internalize pathogens has been fairly established. In activated DC, which constitute the most potent antigen-presenting cells of the immune system, RhoA is also important for the presentation of pathogen-derived antigen and the formation of an immunological synapse between DC and antigen-specific T cells as a prerequisite to induce adaptive T cell responses. In T cells and B cells as the effector cells of the adaptive immune system Rho signaling is pivotal for activation and migration. More recently, mutations of Rho and Rho-modulating factors have been identified to predispose for autoimmune diseases and as causative for hematopoietic malignancies.

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The ability of taxanes to activate RhoA can be relevant for understanding their efficacy in cancer therapy, because RhoA can promote anti-tumour immune responses.
“The ability of taxanes to activate RhoA can be relevant for understanding their efficacy in cancer therapy, because RhoA can promote anti-tumour immune responses 19,75,76 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [75]
Section 3.2 describes RhoA’s role in T-cell activation and migration, supporting the general point that RhoA can facilitate immune responses. Section 3.1 mentions anti-tumour immune responses, but does not establish that RhoA promotes them; the paper also does not link taxane-induced RhoA activation to cancer-treatment efficacy. The taxane-activation point may be covered by the sentence’s other citations. (LLM, conf=0.80)
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Franke, A., McGovern, D. P. B., Barrett, J. C., Wang, K., Radford-Smith, G. L., Ahmad, T., Lees, C. W., Balschun, T., Lee, J., Roberts, R., et al. (2010) · Nature Genetics · doi:10.1038/ng.717 · Cited by 2,520 · see citing works
Rho GTPases and their effector proteins
Bishop, A. L., & Hall, A. (2000) · Biochemical Journal · doi:10.1042/bj3480241 · Cited by 2,040 · see citing works
Multiple Sclerosis: An Immune or Neurodegenerative Disorder?
Trapp, B. D., & Nave, K.-A. (2008) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.30.051606.094313 · Cited by 1,724 · see citing works
Role of Human Macrophage Polarization in Inflammation during Infectious Diseases
Atri, C., Guerfali, F. Z., & Laouini, D. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19061801 · Cited by 1,287 · see citing works
Human autoimmune diseases: a comprehensive update
Wang, L., Wang, F., & Gershwin, M. E. (2015) · Journal of Internal Medicine · doi:10.1111/joim.12395 · Cited by 1,201 · see citing works
Pathogenic conversion of Foxp3+ T cells into TH17 cells in autoimmune arthritis
Komatsu, N., Okamoto, K., Sawa, S., Nakashima, T., Oh-hora, M., Kodama, T., Tanaka, S., Bluestone, J. A., & Takayanagi, H. (2014) · Nature Medicine · doi:10.1038/nm.3432 · Cited by 1,153 · see citing works
Pathological mechanisms in progressive multiple sclerosis
Mahad, D., Trapp, B. D., & Lassmann, H. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70256-x · Cited by 1,147 · see citing works
Identification of 15 new psoriasis susceptibility loci highlights the role of innate immunity
Collaborative Association Study of Psoriasis (CASP), Tsoi, L. C., Genetic Analysis of Psoriasis Consortium, Psoriasis Association Genetics Extension, Wellcome Trust Case Control Consortium 2, Spain, S. L., Knight, J., Ellinghaus, E., Stuart, P. E., Capon, F., et al. (2012) · Nature Genetics · doi:10.1038/ng.2467 · Cited by 1,024 · see citing works
Novel Markers to Delineate Murine M1 and M2 Macrophages
Jablonski, K., Amici, S. A., Webb, L., Ruiz‐Rosado, J. D. D., Popovich, P. G., Partida‐Sánchez, S., & Guerau‐de‐Arellano, M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145342 · Cited by 1,003 · see citing works
The interface between innate and adaptive immunity
Hoebe, K. H. N., Janssen, E. M., & Beutler, B. (2004) · Nature Immunology · doi:10.1038/ni1004-971 · Cited by 919 · see citing works
Regulating Rho GTPases and their regulators
Hodge, R. G., & Ridley, A. J. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.67 · Cited by 903 · see citing works
Innate immune sensing of bacterial modifications of Rho GTPases by the Pyrin inflammasome
Xu, H., Yang, J., Gao, W., Li, L., Li, P., Zhang, L., Gong, Y., Peng, X., Xi, J., Chen, S., et al. (2014) · Nature · doi:10.1038/nature13449 · Cited by 852 · see citing works
Dendritic Cells: Translating Innate to Adaptive Immunity
Steinman, R. M., & Hemmi, H. (2006) · Springer eBooks · doi:10.1007/3-540-32636-7_2 · Cited by 844 · see citing works
Shared and Distinct Genetic Variants in Type 1 Diabetes and Celiac Disease
Smyth, D. J., Plagnol, V., Walker, N. M., Cooper, J. D., Downes, K., Yang, J. H. M., Howson, J. M. M., Stevens, H. E., McManus, R., Wijmenga, C., et al. (2008) · New England Journal of Medicine · doi:10.1056/nejmoa0807917 · Cited by 738 · see citing works
1,25-Dihydroxyvitamin D3 reversibly blocks the progression of relapsing encephalomyelitis, a model of multiple sclerosis.
Cantorna, M. T., Hayes, C. E., & DeLuca, H. F. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.7861 · Cited by 720 · see citing works
Divergent Signals and Cytoskeletal Assemblies Regulate Self-Organizing Polarity in Neutrophils
Xu, J., Wang, F., Keymeulen, A. V., Herzmark, P., Straight, A. F., Kelly, K., Takuwa, Y., Sugimoto, N., Mitchison, T. J., & Bourne, H. R. (2003) · Cell · doi:10.1016/s0092-8674(03)00555-5 · Cited by 687 · see citing works
Newly identified genetic risk variants for celiac disease related to the immune response
Hunt, K. A., Zhernakova, A., Turner, G., Heap, G., Franke, L., Bruinenberg, M., Romanos, J., Dinesen, L. C., Ryan, A. W., Panesar, D., et al. (2008) · Nature Genetics · doi:10.1038/ng.102 · Cited by 675 · see citing works
Type 2 cytokines: mechanisms and therapeutic strategies
Wynn, T. A. (2015) · Nature reviews. Immunology · doi:10.1038/nri3831 · Cited by 671 · see citing works
Peripheral CD4+ T‐cell differentiation regulated by networks of cytokines and transcription factors
Zhu, J., & Paul, W. E. (2010) · Immunological Reviews · doi:10.1111/j.1600-065x.2010.00951.x · Cited by 596 · see citing works
Pyrin inflammasome activation and RhoA signaling in the autoinflammatory diseases FMF and HIDS
Park, Y. H., Wood, G., Kastner, D. L., & Chae, J. J. (2016) · Nature Immunology · doi:10.1038/ni.3457 · Cited by 584 · see citing works
Rho-associated coiled-coil containing kinases (ROCK): Structure, regulation, and functions
Julian, L., & Olson, M. F. (2014) · Small GTPases · doi:10.4161/sgtp.29846 · Cited by 550 · see citing works
Macrophages in wound healing: activation and plasticity
Kim, S. Y., & Nair, M. G. (2019) · Immunology and Cell Biology · doi:10.1111/imcb.12236 · Cited by 536 · see citing works
Regulation of PTEN by Rho small GTPases
Zhong, L., Dong, X., Wang, Z., Liu, W., Deng, N., Ding, Y., Tang, L.-Y., Hla, T., Zeng, R., Li, L., et al. (2005) · Nature Cell Biology · doi:10.1038/ncb1236 · Cited by 488 · see citing works
Interleukin-1 Beta—A Friend or Foe in Malignancies?
Bent, R., Moll, L., Grabbe, S., & Bros, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082155 · Cited by 451 · see citing works
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1,25-Dihydroxyvitamin D3 Ameliorates Th17 Autoimmunity via Transcriptional Modulation of Interleukin-17A
Joshi, S. S., Pantalena, L. C., Liu, X.-K., Gaffen, S., Liu, H., Rohowsky-Kochan, C., Ichiyama, K., Yoshimura, A., Steinman, L., Christakos, S., et al. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05020-11 · Cited by 450 · see citing works
How macrophages deal with death
Lemke, G. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0167-y · Cited by 437 · see citing works
Dendritic Cell Function in Vivo during the Steady State: A Role in Peripheral Tolerance
Steinman, R. M., Hawiger, D., Liu, K., Bonifaz, L. C., Bonnyay, D., Mahnke, K., Iyoda, T., Ravetch, J. V., Dhodapkar, M. V., Inaba, K., et al. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb06029.x · Cited by 427 · see citing works
RhoGDI: multiple functions in the regulation of Rho family GTPase activities
Dovas, A., & Couchman, J. (2005) · Biochemical Journal · doi:10.1042/bj20050104 · Cited by 414 · see citing works
FilGAP, a Rho- and ROCK-regulated GAP for Rac binds filamin A to control actin remodelling
Ohta, Y., Hartwig, J. H., & Stossel, T. P. (2006) · Nature Cell Biology · doi:10.1038/ncb1437 · Cited by 390 · see citing works
Mutational and structural analysis of diffuse large B-cell lymphoma using whole-genome sequencing
Morin, R. D., Mungall, K., Pleasance, E., Mungall, A. J. J., Goya, R., Huff, R. D., Scott, D. W., Ding, J., Roth, A. J. L., Chiu, R., et al. (2013) · Blood · doi:10.1182/blood-2013-02-483727 · Cited by 389 · see citing works
Genome‐wide meta‐analysis identifies novel multiple sclerosis susceptibility loci
Patsopoulos, N. A., the Bayer Pharma MS Genetics Working Group, T. S. C. O. S. E. I. A. A. C., & de Bakker, P. I. W. (2011) · Annals of Neurology · doi:10.1002/ana.22609 · Cited by 353 · see citing works
Genetic variants at CD28, PRDM1 and CD2/CD58 are associated with rheumatoid arthritis risk
Raychaudhuri, S., Thomson, B. P., Remmers, E. F., Eyre, S., Hinks, A., Guiducci, C., Catanese, J. J., ., G. X., Stahl, E. A., Chen, R., et al. (2009) · Nature Genetics · doi:10.1038/ng.479 · Cited by 351 · see citing works
Targeting Th17 cells in autoimmune diseases
Yang, J., Sundrud, M. S., Skepner, J. E., & Yamagata, T. (2014) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2014.07.006 · Cited by 348 · see citing works
Loss of signalling via Gα13 in germinal centre B-cell-derived lymphoma
Muppidi, J. R., Schmitz, R., Green, J. A., Xiao, W., Larsen, A. B., Braun, S. E., An, J., Xu, Y., Rosenwald, A., Ott, G., et al. (2014) · Nature · doi:10.1038/nature13765 · Cited by 298 · see citing works
Cellular Self-Defense: How Cell-Autonomous Immunity Protects Against Pathogens
Randow, F., MacMicking, J. D., & James, L. C. (2013) · Science · doi:10.1126/science.1233028 · Cited by 294 · see citing works
Th17 Cells in Immunity and Autoimmunity
Bedoya, S. K., Lam, B. K., Lau, K., & Larkin, J. (2013) · Clinical and Developmental Immunology · doi:10.1155/2013/986789 · Cited by 278 · see citing works
Dendritic cell subsets
Macri, C., Pang, E. S., Patton, T., & O’Keeffe, M. A. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.12.009 · Cited by 274 · see citing works
Th17 cells in inflammation and autoimmunity
Singh, R. P., Hasan, S., Sharma, S. P., Nagra, S., Yamaguchi, D. T., Wong, D. T., Hahn, B. H., & Hossain, A. (2014) · Autoimmunity Reviews · doi:10.1016/j.autrev.2014.08.019 · Cited by 269 · see citing works
LFA-1 in T Cell Migration and Differentiation
Walling, B. L., & Kim, M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00952 · Cited by 262 · see citing works
Identification of a Bacterial Type III Effector Family with G Protein Mimicry Functions
Alto, N. M., Shao, F., Lazar, C. S., Brost, R. L., Chua, G., Mattoo, S., McMahon, S. A., Ghosh, P., Hughes, T. R., Boone, C. M., et al. (2006) · Cell · doi:10.1016/j.cell.2005.10.031 · Cited by 262 · see citing works
Vitamin D3 Confers Protection from Autoimmune Encephalomyelitis Only in Female Mice
Spach, K. M., & Hayes, C. E. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.6.4119 · Cited by 251 · see citing works
LFA-1-induced T cell migration on ICAM-1 involves regulation of MLCK-mediated attachment and ROCK-dependent detachment
Smith, A. M., Bracke, M., Leitinger, B., Porter, J. C., & Hogg, N. (2003) · Journal of Cell Science · doi:10.1242/jcs.00606 · Cited by 245 · see citing works
The Interplay Between Neutrophils and CD8+ T Cells Improves Survival in Human Colorectal Cancer
Governa, V., Trella, E., Mele, V., Tornillo, L., Amicarella, F., Cremonesi, E., Muraro, M. G., Xu, H., Droeser, R. A., Däster, S., et al. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-16-2047 · Cited by 237 · see citing works
Neutrophils and Immunity: From Bactericidal Action to Being Conquered
Teng, T., Ji, A.-L., Ji, X., & Li, Y. (2017) · Journal of Immunology Research · doi:10.1155/2017/9671604 · Cited by 237 · see citing works
Functions of CD40 and Its Ligand, gp39 (CD40L)
Laman, J. D., Claassen, E., & Noelle, R. J. (2017) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.v37.i2-6.100 · Cited by 229 · see citing works
Accessory Molecule and Costimulation Requirements for CD4 T Cell Response
Croft, M., & Dubey, C. (1997) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.v17.i1.40 · Cited by 227 · see citing works
Regulation of RhoGEF proteins by G 12/13 ‐coupled receptors
Siehler, S. (2009) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2009.00121.x · Cited by 227 · see citing works
β2 Integrins As Regulators of Dendritic Cell, Monocyte, and Macrophage Function
Schittenhelm, L., Hilkens, C. M. U., & Morrison, V. L. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01866 · Cited by 222 · see citing works
Innate control of actin nucleation determines two distinct migration behaviours in dendritic cells
Vargas, P., Maiuri, P., Bretou, M., Sáez, P. J., Pierobon, P., Maurin, M., Chabaud, M., Lankar, D., Obino, D., Terriac, E., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3284 · Cited by 220 · see citing works
RHOA G17V Induces T Follicular Helper Cell Specification and Promotes Lymphomagenesis
Cortés, J. R., Ambesi‐Impiombato, A., Couronné, L., Quinn, S. A., Kim, C. S., Almeida, A. C. D. S., West, Z., Belver, L., Martin, M. S., Scourzic, L., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.01.001 · Cited by 216 · see citing works
Function and mechanism of the pyrin inflammasome
Heilig, R., & Brož, P. (2017) · European Journal of Immunology · doi:10.1002/eji.201746947 · Cited by 206 · see citing works
N -Acetylcysteine: Antioxidant, Aldehyde Scavenger, and More
Zhitkovich, A. (2019) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.9b00152 · Cited by 202 · see citing works
Dia1 and IQGAP1 interact in cell migration and phagocytic cup formation
Brandt, D. T., Marion, S., Griffiths, G. W., Watanabe, T., Kaibuchi, K., & Grosse, R. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612071 · Cited by 199 · see citing works
Tumour-Associated Macrophages (TAMs) in Colon Cancer and How to Reeducate Them
Yahaya, M. A. F., Lila, M. A. M., Ismail, S., Zainol, M., & Rahman, N. M. A. N. A. (2019) · Journal of Immunology Research · doi:10.1155/2019/2368249 · Cited by 187 · see citing works
Rap1 Functions as a Key Regulator of T-Cell and Antigen-Presenting Cell Interactions and Modulates T-Cell Responses
Katagiri, K., Hattori, M., Minato, N., & Kinashi, T. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.4.1001-1015.2002 · Cited by 182 · see citing works
A novel type of myosin implicated in signalling by rho family GTPases.
Reinhard, J., Scheel, A. A., Diekmann, D., Hall, A., Ruppert, C., & Bähler, M. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07048.x · Cited by 180 · see citing works
The cytoskeleton in cell-autonomous immunity: structural determinants of host defence
Mostowy, S., & Shenoy, A. R. (2015) · Nature reviews. Immunology · doi:10.1038/nri3877 · Cited by 175 · see citing works
Rho signaling research: history, current status and future directions
Narumiya, S., & Thumkeo, D. (2018) · FEBS Letters · doi:10.1002/1873-3468.13087 · Cited by 169 · see citing works
The Mst1 and Mst2 kinases control activation of rho family GTPases and thymic egress of mature thymocytes
Mou, F., Praskova, M. D., Xia, F., Buren, D. V., Hock, H. R., Avruch, J., & Zhou, D. (2012) · The Journal of Experimental Medicine · doi:10.1084/jem.20111692 · Cited by 162 · see citing works
Opposite Effects of Rho Family GTPases on Engulfment of Apoptotic Cells by Macrophages
Nakaya, M., Tanaka, M., Okabe, Y., Hanayama, R., & Nagata, S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510972200 · Cited by 155 · see citing works
Epidemiology of Multiple Sclerosis
Ramagopalan, S. V., & Sadovnick, A. D. (2011) · Neurologic Clinics · doi:10.1016/j.ncl.2010.12.010 · Cited by 154 · see citing works
Small GTPases
Reiner, D. J. (2016) · WormBook · doi:10.1895/wormbook.1.67.2 · Cited by 152 · see citing works
Update on the role of alternatively activated macrophages in asthma
Jiang, Z., & Zhu, L. (2016) · Journal of Asthma and Allergy · doi:10.2147/jaa.s104508 · Cited by 151 · see citing works
Cytoskeletal control of B cell responses to antigens
Tolar, P. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.67 · Cited by 148 · see citing works
How neutrophils kill fungi
Gazendam, R. P., van de Geer, A., Roos, D., van den Berg, T. K., & Kuijpers, T. W. (2016) · Immunological Reviews · doi:10.1111/imr.12454 · Cited by 146 · see citing works
Signaling through CD19 activates Vav/mitogen-activated protein kinase pathway and induces formation of a CD19/Vav/phosphatidylinositol 3-kinase complex in human B cell precursors.
Weng, W., Jarvis, L. J., & LeBien, T. W. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31664-8 · Cited by 145 · see citing works
1,25‐Dihydroxyvitamin D3 acts directly on the T lymphocyte vitamin D receptor to inhibit experimental autoimmune encephalomyelitis
Mayne, C. G., Spanier, J. A., Relland, L. M., Williams, C. B., & Hayes, C. E. (2011) · European Journal of Immunology · doi:10.1002/eji.201040632 · Cited by 145 · see citing works
Coordinated RhoA signaling at the leading edge and uropod is required for T cell transendothelial migration
Heasman, S. J., Carlin, L. M., Cox, S., Ng, T., & Ridley, A. J. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201002067 · Cited by 140 · see citing works
Activation of RHOA–VAV1 signaling in angioimmunoblastic T-cell lymphoma
Fujisawa, M., Sakata‐Yanagimoto, M., Nishizawa, S., Komori, D., Gershon, P. D., Kiryu, M., Nuhat, S. T., Fukumoto, K., Enami, T., Muratani, M., et al. (2017) · Leukemia · doi:10.1038/leu.2017.273 · Cited by 138 · see citing works
Macropinocytosis: New Insights Into Its Underappreciated Role in Innate Immune Cell Surveillance
Canton, J. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02286 · Cited by 138 · see citing works
Dasatinib: A Review in Chronic Myeloid Leukaemia and Ph+ Acute Lymphoblastic Leukaemia
Keating, G. M. (2016) · Drugs · doi:10.1007/s40265-016-0677-x · Cited by 136 · see citing works
Chronic lymphocytic leukemia cells induce defective LFA-1–directed T-cell motility by altering Rho GTPase signaling that is reversible with lenalidomide
Ramsay, A. G., Evans, R., Kiaii, S., Svensson, L. M., Hogg, N., & Gribben, J. G. (2013) · Blood · doi:10.1182/blood-2012-08-448332 · Cited by 135 · see citing works
Transforming growth factor-β1 regulates macrophage migration via RhoA
Kim, J.-S., Kim, J.-G., Moon, M.-Y., Jeon, C.-Y., Won, H.-Y., Kim, H.-J., Jeon, Y.-J., Seo, J.-Y., Kim, J.-I., Kim, J., et al. (2006) · Blood · doi:10.1182/blood-2005-10-009191 · Cited by 134 · see citing works
Regulation of RhoA GTPase and various transcription factors in the RhoA pathway
Kim, J., Islam, R., Cho, J. Y., Jeong, H., Cap, K., Park, Y., Hossain, A. J., & Park, J. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.26487 · Cited by 131 · see citing works
Motorized RhoGAP myosin IXb (Myo9b) controls cell shape and motility
Hanley, P. J., Xu, Y., Kronlage, M., Grobe, K., Schön, P. M., Song, J., Sorokin, L. M., Schwab, A., & Bähler, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0911986107 · Cited by 130 · see citing works
Attributes of alternatively activated (M2) macrophages
Shrivastava, R., & Shukla, N. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.03.062 · Cited by 130 · see citing works
CD169+ Macrophages Capture and Dendritic Cells Instruct: The Interplay of the Gatekeeper and the General of the Immune System
Grabowska, J. A., Venegas, M. L., Affandi, A. J., & den Haan, J. M. M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02472 · Cited by 129 · see citing works
Molecular interactions shaping the tetraspanin web
van Deventer, S. J., Dunlock, V.-M. E., & van Spriel, A. B. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160284 · Cited by 126 · see citing works
The role of CR3 (CD11b/CD18) and CR4 (CD11c/CD18) in complement-mediated phagocytosis and podosome formation by human phagocytes
Lukácsi, S., Nagy‐Baló, Z., Erdei, A., Sándor, N., & Bajtay, Z. (2017) · Immunology Letters · doi:10.1016/j.imlet.2017.05.014 · Cited by 125 · see citing works
RhoA G17V is sufficient to induce autoimmunity and promotes T-cell lymphomagenesis in mice
Ng, S. Y., Brown, L., Stevenson, K. E., DeSouza, T., Aster, J. C., Louissaint, A., & Weinstock, D. M. (2018) · Blood · doi:10.1182/blood-2017-11-818617 · Cited by 123 · see citing works
Variegated RHOA mutations in adult T-cell leukemia/lymphoma
Nagata, Y., Kontani, K., Enami, T., Kataoka, K., Ishii, R., Totoki, Y., Kataoka, T. R., Hirata, M., Aoki, K., Nakano, K., et al. (2015) · Blood · doi:10.1182/blood-2015-06-644948 · Cited by 119 · see citing works
Adenylate Cyclase Toxin Subverts Phagocyte Function by RhoA Inhibition and Unproductive Ruffling
Kamanová, J., Kofroňová, O., Mašín, J., Genth, H., Vojtová, J., Linhartová, I., Benada, O., Just, I., & Šebo, P. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.8.5587 · Cited by 118 · see citing works
Phosphatidylinositol (3,4) bisphosphate-specific phosphatases and effector proteins: A distinct branch of PI3K signaling
Li, H., & Marshall, A. J. (2015) · Cellular Signalling · doi:10.1016/j.cellsig.2015.05.013 · Cited by 116 · see citing works
Rac1 links leading edge and uropod events through Rho and myosin activation during chemotaxis
Pestonjamasp, K. N., Forster, C., Sun, C., Gardiner, E. M. M., Bohl, B. P., Weiner, O. D., Bokoch, G., & Glogauer, M. (2006) · Blood · doi:10.1182/blood-2006-01-010363 · Cited by 114 · see citing works
P2X1 Ion Channels Promote Neutrophil Chemotaxis through Rho Kinase Activation
Lecut, C., Frederix, K., Johnson, D. M., Deroanne, C., Thiry, M., Faccinetto, C., Marée, R., Evans, R. J., Volders, P. G. A., Bours, V., et al. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0804007 · Cited by 112 · see citing works
Human myosin-IXb, an unconventional myosin with a chimerin-like rho/rac GTPase-activating protein domain in its tail
Wirth, J. A., Jensen, K. A., Post, P. L., Bement, W. M., & Mooseker, M. S. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.3.653 · Cited by 112 · see citing works
LIM kinases: cofilin and beyond
Prunier, C., Prudent, R., Kapur, R., Sadoul, K., & Lafanéchère, L. (2017) · Oncotarget · doi:10.18632/oncotarget.16978 · Cited by 111 · see citing works
Selective Modulation of TNF–TNFRs Signaling: Insights for Multiple Sclerosis Treatment
Pegoretti, V., Baron, W., Laman, J. D., & Eisel, U. L. M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00925 · Cited by 107 · see citing works
B cell checkpoints in autoimmune rheumatic diseases
Rubin, S. J. S., Bloom, M. S., & Robinson, W. H. (2019) · Nature Reviews Rheumatology · doi:10.1038/s41584-019-0211-0 · Cited by 107 · see citing works
Human myosin-IXb is a mechanochemically active motor and a GAP for rho
Post, P. L., Bokoch, G., & Mooseker, M. S. (1998) · Journal of Cell Science · doi:10.1242/jcs.111.7.941 · Cited by 106 · see citing works
Phosphatidylinositol 4,5‐bisphosphate: Targeted production and signaling
Sun, Y., Thapa, N., Hedman, A. C., & Anderson, R. A. (2013) · BioEssays · doi:10.1002/bies.201200171 · Cited by 106 · see citing works
The Role of Forkhead Box 1 (FOXO1) in the Immune System: Dendritic Cells, T Cells, B Cells, and Hematopoietic Stem Cells
Ortega, A., Feinberg, D. M., Liang, Y., Rossa, C., & Graves, D. T. (2017) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.2017019636 · Cited by 105 · see citing works
Gene expression analysis suggests that 1,25-dihydroxyvitamin D3reverses experimental autoimmune encephalomyelitis by stimulating inflammatory cell apoptosis
Spach, K. M., Pedersen, L. B., Nashold, F. E., Kayo, T., Yandell, B. S., Prolla, T. A., & Hayes, C. E. (2004) · Physiological Genomics · doi:10.1152/physiolgenomics.00003.2004 · Cited by 100 · see citing works
Rho GTPases link cytoskeletal rearrangements and activation processes induced via the tetraspanin CD82 in T lymphocytes
Delaguillaumie, A., Lagaudrière‐Gesbert, C., Popoff, M. R., & Conjeaud, H. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.2.433 · Cited by 99 · see citing works
Differential requirement for ROCK in dendritic cell migration within lymphatic capillaries in steady-state and inflammation
Nitschké, M., Aebischer, D., Abadier, M., Häner, S., Lucic, M., Vigl, B., Luche, H., Fehling, H. J., Biehlmaier, O., Lyck, R., et al. (2012) · Blood · doi:10.1182/blood-2012-03-417923 · Cited by 96 · see citing works
Origin, Organization, Dynamics, and Function of Actin and Actomyosin Networks at the T Cell Immunological Synapse
Hammer, J. A., Wang, J. C., Saeed, M., & Pedrosa, A. T. (2019) · Annual Review of Immunology · doi:10.1146/annurev-immunol-042718-041341 · Cited by 96 · see citing works
The mDial Formin Is Required for Neutrophil Polarization, Migration, and Activation of the LARG/RhoA/ROCK Signaling Axis during Chemotaxis
Shi, Y., Zhang, J., Mullin, M. J., Dong, B., Alberts, A. S., & Siminovitch, K. A. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0803838 · Cited by 92 · see citing works
MST1/MST2 Protein Kinases: Regulation and Physiologic Roles
Galan, J. A., & Avruch, J. (2016) · Biochemistry · doi:10.1021/acs.biochem.6b00763 · Cited by 91 · see citing works
Basic Aspects of T Helper Cell Differentiation
Gagliani, N., & Huber, S. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6548-9_2 · Cited by 91 · see citing works
Cytoskeletal adaptivity regulates T cell receptor signaling
Thauland, T. J., Hu, K. H., Bruce, M. A., & Butte, M. J. (2017) · Science Signaling · doi:10.1126/scisignal.aah3737 · Cited by 89 · see citing works
Targeting the RhoA-ROCK pathway to reverse T-cell dysfunction in SLE
Rozo, C. T., Chinenov, Y. V., Maharaj, R. K., Gupta, S. K., Leuenberger, L., Kirou, K. A., Bykerk, V. P., Goodman, S. M., Salmon, J. E., & Pernis, A. B. (2016) · Annals of the Rheumatic Diseases · doi:10.1136/annrheumdis-2016-209850 · Cited by 88 · see citing works
The origins and non-canonical functions of macrophages in development and regeneration
Théret, M., Mounier, R., & Rossi, F. M. V. (2019) · Development · doi:10.1242/dev.156000 · Cited by 85 · see citing works
Ligand Recognition Specificity of Leukocyte Integrin αMβ2 (Mac-1, CD11b/CD18) and Its Functional Consequences
Podolnikova, N. P., Podolnikov, A. V., Haas, T. A., Lishko, V. K., & Ugarova, T. P. (2015) · Biochemistry · doi:10.1021/bi5013782 · Cited by 83 · see citing works
PDZRhoGEF and myosin II localize RhoA activity to the back of polarizing neutrophil-like cells
Wong, K., Keymeulen, A. V., & Bourne, H. R. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706167 · Cited by 82 · see citing works
Rho GEF Lsc is required for normal polarization, migration, and adhesion of formyl-peptide–stimulated neutrophils
Francis, S. A., Shen, X., Young, J. K., Kaul, P., & Lerner, D. J. (2005) · Blood · doi:10.1182/blood-2005-03-1164 · Cited by 82 · see citing works
Dynamic Regulation of TCR–Microclusters and the Microsynapse for T Cell Activation
Hashimoto, A. S., & Saito, T. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00255 · Cited by 82 · see citing works
Transforming Growth Factor-β1/Smad7 in Intestinal Immunity, Inflammation, and Cancer
Troncone, E., Marafini, I., Stolfi, C., & Monteleone, G. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01407 · Cited by 80 · see citing works
The RhoA Effector mDia Is Induced During T Cell Activation and Regulates Actin Polymerization and Cell Migration in T Lymphocytes
Vicente‐Manzanares, M., Rey, M., Pérez‐Martínez, M., Yáñez‐Mó, M., Sancho, D., Cabrero, J. R., Barreiro, O., de la Fuente, H., Itoh, K., & Sánchez‐Madrid, F. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.2.1023 · Cited by 80 · see citing works
Inactivating mutations in GNA13 and RHOA in Burkitt’s lymphoma and diffuse large B-cell lymphoma: a tumor suppressor function for the Gα13/RhoA axis in B cells
O’Hayre, M., Inoue, A., Kufareva, I., Wang, Z., Mikelis, C. M., Drummond, R. A., Avino, S., Finkel, K., Kalim, K. W., DiPasquale, G., et al. (2015) · Oncogene · doi:10.1038/onc.2015.442 · Cited by 79 · see citing works
Small Rho GTPases Regulate Antigen Presentation in Dendritic Cells
Shurin, G. V., Tourkova, I. L., Chatta, G. S., Schmidt, G., Wei, S., Djeu, J. Y., & Shurin, M. R. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.6.3394 · Cited by 78 · see citing works
Tetraspanin CD151 regulates RhoA activation and the dynamic stability of carcinoma cell-cell contacts
Johnson, J. L., Winterwood, N. E., DeMali, K. A., & Stipp, C. S. (2009) · Journal of Cell Science · doi:10.1242/jcs.045997 · Cited by 77 · see citing works
GEFs: Dual regulation of Rac1 signaling
Marei, H., & Malliri, A. (2016) · Small GTPases · doi:10.1080/21541248.2016.1202635 · Cited by 77 · see citing works
An unappreciated role for neutrophil-DC hybrids in immunity to invasive fungal infections
Fites, J. S., Gui, M., Kernien, J. F., Negoro, P. E., Dagher, Z., Sykes, D. B., Nett, J. E., Mansour, M. K., & Klein, B. S. (2018) · PLoS Pathogens · doi:10.1371/journal.ppat.1007073 · Cited by 76 · see citing works
Tetraspanins CD37 and CD151 differentially regulate Ag presentation and T‐cell co‐stimulation by DC
Sheng, K., van Spriel, A. B., Gartlan, K. H., Sofi, M., Apostolopoulos, V., Ashman, L. K., & Wright, M. D. (2008) · European Journal of Immunology · doi:10.1002/eji.200838798 · Cited by 74 · see citing works
RhoA GTPase Regulates B Cell Receptor Signaling
Saci, A., & Carpenter, C. L. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.12.012 · Cited by 72 · see citing works
A growth factor signaling cascade confined to circular ruffles in macrophages
Welliver, T. P., & Swanson, J. A. (2012) · Biology Open · doi:10.1242/bio.20121784 · Cited by 72 · see citing works
RhoG is required for both FcγR- and CR3-mediated phagocytosis
Tzircotis, G., Braga, V. M. M., & Caron, E. (2011) · Journal of Cell Science · doi:10.1242/jcs.084269 · Cited by 71 · see citing works
The catalytic activity of the kinase ZAP-70 mediates basal signaling and negative feedback of the T cell receptor pathway
Sjolin-Goodfellow, H. E., Frushicheva, M. P., Ji, Q., Cheng, D. A., Kadlecek, T. A., Cantor, A. J., Kuriyan, J., Chakraborty, A. K., Salomon, A. R., & Weiss, A. (2015) · Science Signaling · doi:10.1126/scisignal.2005596 · Cited by 69 · see citing works
Exchange protein directly activated by cAMP encoded by the mammalian rapgef3 gene: Structure, function and therapeutics
Banerjee, U., & Cheng, X. (2015) · Gene · doi:10.1016/j.gene.2015.06.063 · Cited by 68 · see citing works
Integrin Regulation by RhoA in Thymocytes
Vielkind, S., Gallagher-Gambarelli, M., Gomez, M., Hinton, H. J., & Cantrell, D. A. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.1.350 · Cited by 68 · see citing works
LFA-1 Contributes to Signal I of T-Cell Activation and to the Production of Th1 Cytokines
Varga, G., Nippe, N., Balkow, S., Peters, T., Wild, M. K., Seeliger, S., Beissert, S., Krummen, M., Roth, J., Sunderkötter, C. H., et al. (2010) · Journal of Investigative Dermatology · doi:10.1038/jid.2009.398 · Cited by 67 · see citing works
Self-citation
Human in vivo-differentiated monocyte-derived dendritic cells
Tang-Huau, T.-L., & Segura, É. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.02.018 · Cited by 66 · see citing works
Dendritic Cell Motility and T Cell Activation Requires Regulation of Rho-Cofilin Signaling by the Rho-GTPase Activating Protein Myosin IXb
Xu, Y., Pektor, S., Balkow, S., Hemkemeyer, S. A., Liu, Z., Grobe, K., Hanley, P. J., Shen, L., Bros, M., Schmidt, T., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1300695 · Cited by 63 · see citing works
Self-citation
Metalloproteinase MT1-MMP islets act as memory devices for podosome reemergence
Azzouzi, K. E., Wiesner, C., & Linder, S. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201510043 · Cited by 63 · see citing works
IpgB1 and IpgB2, two homologous effectors secreted via the Mxi-Spa type III secretion apparatus, cooperate to mediate polarized cell invasion and inflammatory potential of Shigella flexenri
Hachani, A., Biskri, L., Rossi, G., Marty, A. J., Ménard, R., Sansonetti, P. J., Parsot, C., Nhieu, G. T. V., Bernardini, M. L., & Allaoui, A. (2007) · Microbes and Infection · doi:10.1016/j.micinf.2007.11.011 · Cited by 63 · see citing works
GNA13 loss in germinal center B cells leads to impaired apoptosis and promotes lymphoma in vivo
Healy, J. A., Nugent, A., Rempel, R. E., Moffitt, A. B., Davis, N. S., Jiang, X., Shingleton, J. R., Zhang, J., Love, C., Datta, J., et al. (2016) · Blood · doi:10.1182/blood-2015-07-659938 · Cited by 63 · see citing works
Cytohesin-1 controls the activation of RhoA and modulates integrin-dependent adhesion and migration of dendritic cells
Quast, T., Tappertzhofen, B., Schild, C., Grell, J., Czeloth, N., Förster, R., Alon, R., Fraemohs, L., Dreck, K., Weber, C., et al. (2009) · Blood · doi:10.1182/blood-2008-08-176123 · Cited by 62 · see citing works
The RhoA-ROCK pathway in the regulation of T and B cell responses
Ricker, E., Chowdhury, L., Yi, W., & Pernis, A. B. (2016) · F1000Research · doi:10.12688/f1000research.7522.1 · Cited by 61 · see citing works
SWAP70 Organizes the Actin Cytoskeleton and Is Essential for Phagocytosis
Baranov, M. V., Revelo, N. H., Dingjan, I., Maraspini, R., ter Beest, M., Honigmann, A., & van den Bogaart, G. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.10.021 · Cited by 60 · see citing works
TRIF–GEFH1–RhoB pathway is involved in MHCII expression on dendritic cells that is critical for CD4 T‐cell activation
Kamon, H., Kawabe, T., Kitamura, H., Lee, J., Kamimura, D., Kaisho, T., Akira, S., Iwamatsu, A., Koga, H., Murakami, M., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601286 · Cited by 60 · see citing works
p21-Activated Kinase (PAK) Regulates Cytoskeletal Reorganization and Directional Migration in Human Neutrophils
Itakura, A., Aslan, J. E., Kusanto, B. T., Phillips, K. G., Porter, J. E., Newton, P. K., Nan, X., Insall, R. H., Chernoff, J., & McCarty, O. J. T. (2013) · PLoS ONE · doi:10.1371/journal.pone.0073063 · Cited by 59 · see citing works
Estrogen-related receptor α decreases RHOA stability to induce orientated cell migration
Sailland, J., Tribollet, V., Forcet, C., Billon, C., Barenton, B., Carnesecchi, J., Bachmann, A., Gauthier, K. C., Yu, S., Giguère, V., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1402094111 · Cited by 57 · see citing works
Rho/ROCK and myosin II control the polarized distribution of endocytic clathrin structures at the uropod of moving T lymphocytes
Samaniego, R., Sanchez-Martín, L., Estecha, A., & Sánchez-Mateos, P. (2007) · Journal of Cell Science · doi:10.1242/jcs.006296 · Cited by 57 · see citing works
Kruppel-like Factor 6 Promotes Macrophage-mediated Inflammation by Suppressing B Cell Leukemia/Lymphoma 6 Expression
Kim, G., Das, R., Goduni, L., McClellan, S. A., Hazlett, L. D., & Mahabeleshwar, G. H. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.738617 · Cited by 56 · see citing works
Head of Myosin IX Binds Calmodulin and Moves Processively toward the Plus-end of Actin Filaments
Liao, W., Elfrink, K., & Bähler, M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.101105 · Cited by 56 · see citing works
Coordinated balance of Rac1 and RhoA plays key roles in determining phagocytic appetite
Kim, S.-Y., Kim, S., Bae, D.-J., Park, S., Lee, G.-Y., Park, G.-M., & Kim, I. (2017) · PLoS ONE · doi:10.1371/journal.pone.0174603 · Cited by 56 · see citing works
LFA-1 activity state on dendritic cells regulates contact duration with T cells and promotes T-cell priming
Balkow, S., Heinz, S., Schmidbauer, P., Kolanus, W., Holzmann, B., Grabbe, S., & Laschinger, M. (2010) · Blood · doi:10.1182/blood-2009-05-224428 · Cited by 55 · see citing works
Self-citation
Inhibition of KLF5–Myo9b–RhoA Pathway–Mediated Podosome Formation in Macrophages Ameliorates Abdominal Aortic Aneurysm
Ma, D., Zheng, B., Suzuki, T., Zhang, R., Jiang, C., Bai, D., Yin, W., Yang, Z., Zhang, X., Hou, L., et al. (2017) · Circulation Research · doi:10.1161/circresaha.116.310367 · Cited by 55 · see citing works
Mouse Macrophages Completely Lacking Rho Subfamily GTPases (RhoA, RhoB, and RhoC) Have Severe Lamellipodial Retraction Defects, but Robust Chemotactic Navigation and Altered Motility
Königs, V., Jennings, R., Vogl, T., Horsthemke, M., Bachg, A. C., Xu, Y., Grobe, K., Brakebusch, C., Schwab, A., Bähler, M., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.563270 · Cited by 54 · see citing works
Loss of ARHGEF1 causes a human primary antibody deficiency
Bouafia, A., Lofek, S., Bruneau, J., Chentout, L., Lamrini, H., Trinquand, A., Deau, M., Heurtier, L., Meignin, V., Pïcard, C., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci120572 · Cited by 54 · see citing works
The Role of Formin Tails in Actin Nucleation, Processive Elongation, and Filament Bundling
Vizcarra, C. L., Bor, B., & Quinlan, M. E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.588368 · Cited by 52 · see citing works
Guanine Nucleotide-Binding Proteins of the G12 Family Shape Immune Functions by Controlling CD4+ T Cell Adhesiveness and Motility
Herroeder, S., Reichardt, P., Sassmann, A., Zimmermann, B., Jaeneke, D., Hoeckner, J., Hollmann, M. W., Fischer, K., Vogt, S., Grosse, R., et al. (2009) · Immunity · doi:10.1016/j.immuni.2009.02.010 · Cited by 52 · see citing works
The pyrin inflammasome: from sensing RhoA GTPases-inhibiting toxins to triggering autoinflammatory syndromes
Jamilloux, Y., Magnotti, F., Bélot, A., & Henry, T. (2018) · Pathogens and Disease · doi:10.1093/femspd/fty020 · Cited by 51 · see citing works
BCL6 suppresses RhoA activity to alter macrophage morphology and motility
Pixley, F. J., Xiong, Y., Yu, R. Y.-L., Sahai, E. A., Stanley, E. R., & Ye, B. H. (2005) · Journal of Cell Science · doi:10.1242/jcs.02314 · Cited by 51 · see citing works
Rho Kinases in Autoimmune Diseases
Pernis, A. B., Ricker, E., Weng, C., Rozo, C. T., & Yi, W. (2016) · Annual Review of Medicine · doi:10.1146/annurev-med-051914-022120 · Cited by 50 · see citing works
Ras-related GTPases Rap1 and RhoA Collectively Induce the Phagocytosis of Serum-opsonized Zymosan Particles in Macrophages
Kim, J.-G., Moon, M., Kim, H., Li, Y., Song, D., Kim, J.-S., Lee, J., Kim, J., Kim, S.-C., & Park, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.257634 · Cited by 50 · see citing works
Regulation of Immature Dendritic Cell Migration by RhoA Guanine Nucleotide Exchange Factor Arhgef5
Wang, Z., Kumamoto, Y., Wang, P., Gan, X., Lehmann, D. M., Smrcka, A. V., Cohn, L. E., Iwasaki, A., Li, L., & Wu, D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.047282 · Cited by 50 · see citing works
Hax1 regulates neutrophil adhesion and motility through RhoA
Cavnar, P. J., Berthier, E., Beebe, D. J., & Anna Huttenlocher, A. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201010143 · Cited by 50 · see citing works
SWAP-70 regulates RhoA/RhoB-dependent MHCII surface localization in dendritic cells
Ocaña‐Morgner, C., Wahren, C., & Jessberger, R. (2008) · Blood · doi:10.1182/blood-2008-04-152587 · Cited by 49 · see citing works
Postthymic maturation influences the CD8 T cell response to antigen
Makaroff, L., Hendricks, D. W., Niec, R. E., & Fink, P. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812354106 · Cited by 49 · see citing works
Rac‐ GTP ases and Rac‐ GEF s in neutrophil adhesion, migration and recruitment
Pantarelli, C., & Welch, H. C. E. (2018) · European Journal of Clinical Investigation · doi:10.1111/eci.12939 · Cited by 48 · see citing works
Autotaxin Produced by Stromal Cells Promotes LFA-1–Independent and Rho-Dependent Interstitial T Cell Motility in the Lymph Node Paracortex
Katakai, T., Kondo, N., Ueda, Y., & Kinashi, T. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1400565 · Cited by 48 · see citing works
Fam65b Is a New Transcriptional Target of FOXO1 That Regulates RhoA Signaling for T Lymphocyte Migration
Rougerie, P., Largeteau, Q., Megrelis, L., Carrette, F., Lejeune, T., Toffali, L., Rossi, B., Zeghouf, M., Cherfils, J., Constantin, G., et al. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1201174 · Cited by 48 · see citing works
Discoidin domain receptor 1 promotes Th17 cell migration by activating the RhoA/ROCK/MAPK/ERK signaling pathway
Azreq, M.-A. E., Kadiri, M., Boisvert, M., Pagé, N., Tessier, P. A., & Aoudjit, F. (2016) · Oncotarget · doi:10.18632/oncotarget.10455 · Cited by 48 · see citing works
Absence of PI3Kγ leads to increased leukocyte apoptosis and diminished severity of experimental autoimmune encephalomyelitis
Rodrigues, D. H., Vilela, M. C., Barcelos, L. S., Pinho, V., Teixeira, M. M., & Teixeira, A. L. (2010) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2010.02.016 · Cited by 47 · see citing works
RhoA of the Rho Family Small GTPases Is Essential for B Lymphocyte Development
Zhang, S., Zhou, X., Lang, R. A., & Guo, F. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033773 · Cited by 47 · see citing works
The Vav Family: At the Crossroads of Signaling Pathways
Swat, W., & Fujikawa, K. (2005) · Immunologic Research · doi:10.1385/ir:32:1-3:259 · Cited by 47 · see citing works
Dendritic Cell Migration and Antigen Presentation Are Coordinated by the Opposing Functions of the Tetraspanins CD82 and CD37
Jones, E. L., Wee, J. L. K., Demaria, M. C., Blakeley, J., Ho, P. K., Vega‐Ramos, J., Villadangos, J. A., van Spriel, A. B., Hickey, M. J., Hämmerling, G. J., et al. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1500357 · Cited by 46 · see citing works
Modular regulation of Rho family GTPases in development
Denk-Lobnig, M., & Martin, A. C. (2017) · Small GTPases · doi:10.1080/21541248.2017.1294234 · Cited by 45 · see citing works
Plasma Membrane Organization Is Essential for Balancing Competing Pseudopod- and Uropod-promoting Signals during Neutrophil Polarization and Migration
Bodin, S., & Welch, M. D. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-04-0358 · Cited by 44 · see citing works
BIG1 Is a Binding Partner of Myosin IXb and Regulates Its Rho-GTPase Activating Protein Activity
Saeki, N., Tokuo, H., & Ikebe, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413415200 · Cited by 43 · see citing works
JAK tyrosine kinases promote hierarchical activation of Rho and Rap modules of integrin activation
Montresor, A., Bolomini‐Vittori, M., Toffali, L., Rossi, B., Constantin, G., & Laudanna, C. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201303067 · Cited by 43 · see citing works
Defective Chemokine-Directed Lymphocyte Migration and Development in the Absence of Rho Guanosine Diphosphate-Dissociation Inhibitors α and β
Ishizaki, H., Togawa, A., Tanaka, M., HORI, K., Nishimura, M., Hamaguchi, A., Imai, T., Takai, Y., & Miyoshi, J. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.12.8512 · Cited by 43 · see citing works
Autotaxin-LPA Axis Regulates hMSC Migration by Adherent Junction Disruption and Cytoskeletal Rearrangement Via LPAR1/3-Dependent PKC/GSK3β/β-Catenin and PKC/Rho GTPase Pathways
Ryu, J. M., & Han, H. J. (2014) · Stem Cells · doi:10.1002/stem.1882 · Cited by 41 · see citing works
RhoA/ROCK/PTEN signaling is involved in AT-101-mediated apoptosis in human leukemia cells in vitro and in vivo
Li, G., Liu, L., Shan, C., Cheng, Q., Budhraja, A., Zhou, T., Cui, H., & Gao, N. (2014) · Cell Death and Disease · doi:10.1038/cddis.2013.519 · Cited by 41 · see citing works
RhoA Is Involved in LFA-1 Extension Triggered by CXCL12 but Not in a Novel Outside-In LFA-1 Activation Facilitated by CXCL9
Pasvolsky, R., Grabovsky, V., Giagulli, C., Shulman, Z., Shamri, R., Feigelson, S. W., Laudanna, C., & Alon, R. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.180.5.2815 · Cited by 41 · see citing works
Phosphorylation-mediated regulation of GEFs for RhoA
Patel, M. R., & Karginov, A. V. (2013) · Cell Adhesion & Migration · doi:10.4161/cam.28058 · Cited by 39 · see citing works
Allosteric regulation of Arf GTPases and their GEFs at the membrane interface
Nawrotek, A., Zeghouf, M., & Cherfils, J. (2016) · Small GTPases · doi:10.1080/21541248.2016.1215778 · Cited by 39 · see citing works
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Badr, G. (2005) · International Immunology · doi:10.1093/intimm/dxh227 · Cited by 39 · see citing works
MYO9B gene polymorphisms are associated with autoimmune diseases in Spanish population
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Sphingosine 1-Phosphate–Induced Motility and Endocytosis of Dendritic Cells Is Regulated by SWAP-70 through RhoA
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Dendritic cells regulate T-cell deattachment through the integrin-interacting protein CYTIP
Hofer, S., Pfeil, K., Niederegger, H., Ebner, S., Nguyen, V. A., Kremmer, E., Auffinger, M., Neyer, S., Fürhapter, C., & Heufler, C. (2005) · Blood · doi:10.1182/blood-2005-01-0425 · Cited by 38 · see citing works
Gene Targeting RhoA Reveals Its Essential Role in Coordinating Mitochondrial Function and Thymocyte Development
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Steffen, A., Stradal, T. E. B., & Rottner, K. (2016) · Handbook of experimental pharmacology · doi:10.1007/164_2016_35 · Cited by 26 · see citing works
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Matsusaka, S., Tohyama, Y., He, J., Shi, Y., Hazama, R., Kadono, T., Kurihara, R., Tohyama, K., & Yamamura, H. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.01.076 · Cited by 26 · see citing works
The small Rho GTPase Rif and actin cytoskeletal remodelling
Fan, L., & Mellor, H. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110625 · Cited by 26 · see citing works

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Komatsu, M., Ichikawa, H., Chiwaki, F., Sakamoto, H., Komatsuzaki, R., Asaumi, M., Tsunoyama, K., Fukagawa, T., Matsushita, H., Boku, N., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02469-6 · Cited by 21 · see citing works
Understanding the erectile dysfunction–cardiovascular disease connection: clinical and pathophysiological insights
An, J., Xiang, B., Peng, J., & Li, D. (2025) · Sexual Medicine Reviews · doi:10.1093/sxmrev/qeaf014 · Cited by 20 · see citing works
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Kloc, M., Uosef, A., Villagrán, M., Zdanowski, R., Kubiak, J. Z., Wosik, J., & Ghobrial, R. M. (2021) · Biology · doi:10.3390/biology10020070 · Cited by 20 · see citing works
Systemic barrier dysfunction in type 2 inflammation diseases: perspective in the skin, airways, and gastrointestinal tract
Meng, J., Xiao, H., Xu, F., She, X., Liu, C., & Canonica, G. W. (2025) · Immunologic Research · doi:10.1007/s12026-025-09606-9 · Cited by 21 · see citing works
TAGAP activates Th17 cell differentiation by promoting RhoA and NLRP3 to accelerate rheumatoid arthritis development
Sun, H., Jiang, Q., Fan, W., Shen, X.-Y., Wang, Z., & Wang, X. (2023) · Clinical & Experimental Immunology · doi:10.1093/cei/uxad084 · Cited by 19 · see citing works
Rho GTPase signaling in rheumatic diseases
Zeng, R., Zhuo, Z., Luo, Y., Sha, W., & Chen, H. H. (2021) · iScience · doi:10.1016/j.isci.2021.103620 · Cited by 19 · see citing works
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Que, F., Zhang, L., Wang, T., Xu, M., Li, W., & Zang, S. (2022) · OncoImmunology · doi:10.1080/2162402x.2022.2134536 · Cited by 18 · see citing works
Role of ROCK signaling in virus replication
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Ding, Y., Fang, F., Liu, X., Sheng, S., Li, X., Yin, X., Chen, Z., & Wen, J. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03797-8 · Cited by 18 · see citing works
Elimination of Aicardi–Goutières syndrome protein SAMHD1 activates cellular innate immunity and suppresses SARS-CoV-2 replication
Oo, A., Zandi, K., Shepard, C., Bassit, L., Musall, K., Goh, S. L., Cho, Y., Kim, D., Schinazi, R. F., & Kim, B. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101635 · Cited by 18 · see citing works
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Brakebusch, C. (2021) · Cells · doi:10.3390/cells10020401 · Cited by 18 · see citing works
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Kilian, L. S., Frank, D., & Rangrez, A. Y. (2021) · Cells · doi:10.3390/cells10071681 · Cited by 17 · see citing works
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Tameni, A., Sauta, E., Mularoni, V., Torricelli, F., Manzotti, G., Inghirami, G., Bellazzi, R., Fragliasso, V., & Ciarrocchi, A. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03425-0 · Cited by 17 · see citing works
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Joshua, J., Caswell, J., O’Sullivan, M. L., Wood, G. A., & Fonfara, S. (2023) · PLoS ONE · doi:10.1371/journal.pone.0283244 · Cited by 15 · see citing works
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Zhang, Y., Zhou, X., Zhong, Y., Chen, X. X., Li, Z., Li, R., Qin, P., Wang, S., Yin, J., Liu, S., et al. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad187 · Cited by 15 · see citing works
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Asfor, A. S., Nazki, S., Reddy, V. R. A. P., Campbell, E. A., Dulwich, K. L., Giotis, E. S., Skinner, M. A., & Broadbent, A. (2021) · Viruses · doi:10.3390/v13050933 · Cited by 15 · see citing works
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Chen, L., Cheng, B., Yang, Z., Zheng, M., Chu, T. W., Wang, P., He, T., Xue, Y., Ren, H., Zheng, L., et al. (2025) · National Science Review · doi:10.1093/nsr/nwaf256 · Cited by 14 · see citing works
Interplay of G-proteins and Serotonin in the Neuroimmunoinflammatory Model of Chronic Stress and Depression: A Narrative Review
Gusev, E., & Sarapultsev, A. (2023) · Current Pharmaceutical Design · doi:10.2174/0113816128285578231218102020 · Cited by 15 · see citing works
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Self-citation
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Retracted
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Domingos, C., Müller, F. E., Passlick, S., Wachten, D., Ponimaskin, E. G., Schwarz, M. K., Schoch, S., Zeug, A., & Henneberger, C. (2023) · Cells · doi:10.3390/cells12020331 · Cited by 9 · see citing works
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Gajardo, T., Bernard, M., Lô, M., Turck, E., Leveau, C., El‐Daher, M., Deslys, A., Panikulam, P., Menche, C., Kurowska, M., et al. (2023) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2023.06.016 · Cited by 9 · see citing works
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Soobryan, N., Reddy, K., Ibrahim, U. H., Moodley, J., Kumar, A., & Mackraj, I. (2023) · Placenta · doi:10.1016/j.placenta.2023.11.011 · Cited by 9 · see citing works
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Fellermann, M., Huchler, C., Fechter, L., Kolb, T., Wondany, F., Mayer, D., Michaelis, J., Stenger, S., Mellert, K., Möller, P., et al. (2020) · Toxins · doi:10.3390/toxins12090563 · Cited by 9 · see citing works
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Lee, J., Choi, S.-Y., Park, S.-Y., Jung, N.-C., Noh, K.-E., Nam, J.-H., Oh, J.-S., Choi, H., Jang, J.-S., Yoo, J. Y., et al. (2021) · Biomedicines · doi:10.3390/biomedicines9111727 · Cited by 9 · see citing works

The RhoA-ROCK pathway in the regulation of T and B cell responses
Ricker, E., Chowdhury, L., Yi, W., & Pernis, A. B. (2016) · F1000Research · doi:10.12688/f1000research.7522.1 · Cited by 61 · see citing works
Role of RhoG as a regulator of cellular functions: integrating insights on immune cell activation, migration, and functions
Kumar, S., Singh, D. R., & Sarangi, P. P. (2023) · Inflammation Research · doi:10.1007/s00011-023-01761-9 · Cited by 12 · see citing works
Small Rho GTPases Regulate Antigen Presentation in Dendritic Cells
Shurin, G. V., Tourkova, I. L., Chatta, G. S., Schmidt, G., Wei, S., Djeu, J. Y., & Shurin, M. R. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.6.3394 · Cited by 78 · see citing works
Rho GTPases: Masters of T lymphocyte migration and activation
Rougerie, P., & Delon, J. (2011) · Immunology Letters · doi:10.1016/j.imlet.2011.12.003 · Cited by 85 · see citing works
Dendritic Cell Motility and T Cell Activation Requires Regulation of Rho-Cofilin Signaling by the Rho-GTPase Activating Protein Myosin IXb
Xu, Y., Pektor, S., Balkow, S., Hemkemeyer, S. A., Liu, Z., Grobe, K., Hanley, P. J., Shen, L., Bros, M., Schmidt, T., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1300695 · Cited by 63 · see citing works
Self-citation

Authors: Bros, M., Haas, K., Moll, L., & Grabbe, S.
Affiliations: University Medical Center of the Johannes Gutenberg University Mainz (DE)
Corresponding author: Bros, Matthias
ORCID: Bros, Matthias
Moll, Lorna
Grabbe, Stephan
Venue: Cells
Publisher: MDPI AG
Published: 2019-07-17
Volume: 8
Issue: 7
Pages: 733
ISSN: 2073-4409 (ISSN-L)
DOI: 10.3390/cells8070733
PMC: PMC6678964
OpenAlex: W2959814266
Cited by: 193
References: 234
Citations by year: 2026: 16 · 2025: 19 · 2024: 28 · 2023: 36 · 2022: 27 · 2021: 44 · 2020: 19 · 2019: 2 · 2018: 2
FWCI: 2.03
Type: journal article
Language: en
Open access: gold
dx.doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Cells (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Deutsche Forschungsgemeinschaft (TR156, B01)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Health Sciences › Medicine › Oncology › Chemokine receptors and signaling
Keywords: RhoA, small GTPases, innate immunity, adaptive immunity, neutrophils, macrophages, dendritic cells, immunological synapse, T cell activation, B cell activation, cell migration, cytoskeleton, Rho GTPase signaling, autoimmune disease, hematologic malignancies, antigen presentation
MeSH terms: Animals, Cell Differentiation, Humans, Immunity, Innate, Signal Transduction, rhoA GTP-Binding Protein, Adaptive Immunity

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RhoA as a Key Regulator of Innate and Adaptive Immunity

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