The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Haematopoietic cell-specific CDM family protein DOCK2 is essential for lymphocyte migration
Abstract
Cell migration is a fundamental biological process involving membrane polarization and cytoskeletal dynamics, both of which are regulated by Rho family GTPases. Among these molecules, Rac is crucial for generating the actin-rich lamellipodial protrusion, a principal part of the driving force for movement. The CDM family proteins, Caenorhabditis elegans CED-5, human DOCK180 and Drosophila melanogaster Myoblast City (MBC), are implicated to mediate membrane extension by functioning upstream of Rac. Although genetic analysis has shown that CED-5 and Myoblast City are crucial for migration of particular types of cells, physiological relevance of the CDM family proteins in mammals remains unknown. Here we show that DOCK2, a haematopoietic cell-specific CDM family protein, is indispensable for lymphocyte chemotaxis. DOCK2-deficient mice (DOCK2-/-) exhibited migration defects of T and B lymphocytes, but not of monocytes, in response to chemokines, resulting in several abnormalities including T lymphocytopenia, atrophy of lymphoid follicles and loss of marginal-zone B cells. In DOCK2-/- lymphocytes, chemokine-induced Rac activation and actin polymerization were almost totally abolished. Thus, in lymphocyte migration DOCK2 functions as a central regulator that mediates cytoskeletal reorganization through Rac activation.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“DOCK2 activates Rac but not Cdc42, whereas DOCK9 activates Cdc42 but not Rac (6,35,38).”
From Specific Recognition of Rac2 and Cdc42 by DOCK2 and DOCK9 Guanine Nucleotide Exchange Factors (2008) · cites this paper as [6]
In the citing paper
“Interestingly, the physiological activation of Rac by these GEFs requires their association with a regulatory protein ELMO1 (Engulfment and Motility) (6,33,34).”
From Specific Recognition of Rac2 and Cdc42 by DOCK2 and DOCK9 Guanine Nucleotide Exchange Factors (2008) · cites this paper as [6]
Citations
Cites
Rho GTPases and the Actin Cytoskeleton
Hall, A. (1998) · Science · doi:10.1126/science.279.5350.509 · Cited by 6,138
Cell Migration: A Physically Integrated Molecular Process
Lauffenburger, D. A., & Horwitz, A. F. (1996) · Cell · doi:10.1016/s0092-8674(00)81280-5 · Cited by 3,915
Förster, R., Schubel, A., Breitfeld, D., Kremmer, E., Renner‐Müller, I., Wolf, E., & Lipp, M. (1999) · Cell · doi:10.1016/s0092-8674(00)80059-8 · Cited by 2,348
The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry
Bleul, C. C., Farzan, M., Choe, H., Parolin, C., Clark‐Lewis, I., Sodroski, J., & Springer, T. A. (1996) · Nature · doi:10.1038/382829a0 · Cited by 1,953
Oberlin, E., Amara, A., Bachelerie, F., Chable-Bessia, C., Virelizier, J., Arenzana‐Seisdedos, F., Schwartz, O., Heard, J., Clark‐Lewis, I., Legler, D. F., et al. (1996) · Nature · doi:10.1038/382833a0 · Cited by 1,652
A brain serine/threonine protein kinase activated by Cdc42 and Rac1
Manser, E. J., Leung, T., Salihuddin, H., Zhao, Z.-S., & Lim, L. (1994) · Nature · doi:10.1038/367040a0 · Cited by 1,541
Central Role for G Protein-Coupled Phosphoinositide 3-Kinase γ in Inflammation
Hirsch, E., Katanaev, V. L., Garlanda, C., Azzolino, O., Pirola, L., Silengo, L., Sozzani, S., Mantovani, A., Altruda, F., & Wymann, M. P. (2000) · Science · doi:10.1126/science.287.5455.1049 · Cited by 1,209
Förster, R., Mattis, A. E., Kremmer, E., Wolf, E., Brem, G., & Lipp, M. (1996) · Cell · doi:10.1016/s0092-8674(00)81798-5 · Cited by 1,129
Function of PI3Kγ in Thymocyte Development, T Cell Activation, and Neutrophil Migration
Sasaki, T., Irie-Sasaki, J., Jones, R. G., Oliveira-dos-Santos, A., Stanford, W. L., Bolon, B. N., Wakeham, A. C., Itié, A., Bouchard, D., Kozieradzki, I., et al. (2000) · Science · doi:10.1126/science.287.5455.1040 · Cited by 1,027
Gunn, M. D., Kyuwa, S., Tam‐Amersdorfer, C., Kakiuchi, T., Matsuzawa, A., Williams, L. T., & Nakano, H. (1999) · The Journal of Experimental Medicine · doi:10.1084/jem.189.3.451 · Cited by 1,019
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 448
In Vitro Guanine Nucleotide Exchange Activity of DHR‐2/DOCKER/CZH2 Domains
Côté, J., & Vuori, K. (2006) · Methods in Enzymology · doi:10.1016/s0076-6879(06)06004-6 · Cited by 45
Cholesterol sulfate is a DOCK2 inhibitor that mediates tissue-specific immune evasion in the eye
Sakurai, T., Uruno, T., Sugiura, Y., Tatsuguchi, T., Yamamura, K., Ushijima, M., Hattori, Y., Kukimoto‐Niino, M., Mishima-Tsumagari, C., Watanabe, M., et al. (2018) · Science Signaling · doi:10.1126/scisignal.aao4874 · Cited by 44
Self-citationKong, M., Bui, T. V., Ditsworth, D., Gruber, J. J., Goncharov, D., Krymskaya, V. P., Lindsten, T., & Thompson, C. B. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703159200 · Cited by 43
Margaron, Y., Fradet, N., & Côté, J. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.431825 · Cited by 45
The Actin-Bundling Protein L-Plastin Is Essential for Marginal Zone B Cell Development
Todd, E. M., Deady, L. E., & Morley, S. C. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1101033 · Cited by 44
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 44
Parameswaran, N., Matsui, K., & Gupta, N. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1001139 · Cited by 45
The emerging role of guanine nucleotide exchange factors in ALS and other neurodegenerative diseases
Droppelmann, C. A., Campos‐Melo, D., Volkening, K., & Strong, M. J. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00282 · Cited by 42
García‐Bernal, D., Sotillo-Mallo, E., Nombela‐Arrieta, C., Samaniego, R., Fukui, Y., Stein, J. V., & Teixidó, J. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.8.5215 · Cited by 41
Self-citationDedicator of Cytokinesis 2 in Cell Signaling Regulation and Disease Development
Guo, X., & Chen, S. (2016) · Journal of Cellular Physiology · doi:10.1002/jcp.25512 · Cited by 40
The small GTPase Ral mediates SDF-1–induced migration of B cells and multiple myeloma cells
de Gorter, D. J. J., Reijmers, R. M., Beuling, E. A., Naber, H. P. H., Kuil, A., Kersten, M. J., Pals, S. T., & Spaargaren, M. (2008) · Blood · doi:10.1182/blood-2007-08-106583 · Cited by 40
Matsuda, T., Yanase, S., Takaoka, A., & Maruyama, M. (2015) · Immunity & Ageing · doi:10.1186/s12979-015-0028-x · Cited by 39
A Chemoattractant-Guided Walk Through Lymphopoiesis
Lim, V., Zehentmeier, S., Fistonich, C., & Pereira, J. P. (2017) · Advances in immunology · doi:10.1016/bs.ai.2017.02.001 · Cited by 40
DOCK8 Immune Deficiency as a Model for Primary Cytoskeletal Dysfunction
McGhee, S. A., & Chatila, T. A. (2010) · Disease Markers · doi:10.1155/2010/397291 · Cited by 40
Smith, L. D., Hickman, E. S., Parry, R. V., Westwick, J. K., & Ward, S. G. (2007) · Cellular Signalling · doi:10.1016/j.cellsig.2007.08.006 · Cited by 38
Wang, J., Xu, L., Shaheen, S., Liu, S., Zheng, W., Sun, X., Li, Z., & Liu, W. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.117 · Cited by 38
DOCK2 Is Required in T Cell Precursors for Development of Vα14 NK T Cells
Kunisaki, Y., Tanaka, Y., Sanui, T., Inayoshi, A., Noda, M., Nakayama, T., Harada, M., Taniguchi, M., Sasazuki, T., & Fukui, Y. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.176.8.4640 · Cited by 37
Self-citationSpecific Recognition of Rac2 and Cdc42 by DOCK2 and DOCK9 Guanine Nucleotide Exchange Factors
Kwofie, M. A., & Skowronski, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705170200 · Cited by 36
Suzuki, E., Williams, S. V., Sato, S., Gilkeson, G. S., Watson, D. K., & Zhang, X. K. (2013) · Immunology · doi:10.1111/imm.12070 · Cited by 36
Cimino, P. J., Yang, Y., Li, X., Hemingway, J. F., Cherne, M. K., Khademi, S. B., Fukui, Y., Montine, K. S., Montine, T. J., & Keene, C. D. (2013) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2013.01.002 · Cited by 36
Self-citationMarginal Zone B Cell Physiology and Disease
Carvalho, T. L., & Kearney, J. F. (2004) · KARGER eBooks · doi:10.1159/000082100 · Cited by 36
Rieken, S., Herroeder, S., Sassmann, A., Wallenwein, B., Moers, A., Offermanns, S., & Wettschureck, N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605287200 · Cited by 36
Xu, X., Su, Y., Wu, K., Pan, F., & Wang, A. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.114399 · Cited by 38
Two‐photon imaging of effector T‐cell behavior: lessons from a tumor model
Ng, L. G., Mrass, P., Kinjyo, I., Reiner, S. L., & Weninger, W. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00596.x · Cited by 36
Chemokines CCL19 and CCL21 promote activation-induced cell death of antigen-responding T cells
Yasuda, T., Kuwabara, T., Nakano, H., Aritomi, K., Onodera, T., Lipp, M., Takahama, Y., & Kakiuchi, T. (2006) · Blood · doi:10.1182/blood-2006-04-018101 · Cited by 35
Prates, I., Penna, A., Rodrigues, M. T., & Carnaval, A. C. (2018) · Ecology and Evolution · doi:10.1002/ece3.4650 · Cited by 35
Arai, A., Jin, A., Weihua, Y., Mizuchi, D., Yamamoto, K., Nanki, T., & Miura, O. (2004) · Cellular Signalling · doi:10.1016/j.cellsig.2004.09.007 · Cited by 35
Cho, H., & Kehrl, J. H. (2009) · Progress in molecular biology and translational science · doi:10.1016/s1877-1173(09)86009-2 · Cited by 34
Xia, J., Yuan, J., Xin, L., Zhang, Y., Kong, S., Chen, Y., Yang, S., & Li, K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113724 · Cited by 35
Tachibana, M., Kiyokawa, E., Hara, S., Iemura, S.-I., Natsume, T., Manabe, T., & Matsuda, M. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.12.005 · Cited by 36
Ayensu, W. K., & Tchounwou, P. B. (2006) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph2006030018 · Cited by 34
Viau, M., Longo, N. S., Lipsky, P. E., & Zouali, M. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.11.7719 · Cited by 34
Chemokines and other mediators in the development and functional organization of lymph nodes
Eckert, N., Permanyer, M., Yu, K., Werth, K., & Förster, R. (2019) · Immunological Reviews · doi:10.1111/imr.12746 · Cited by 34
Schaecher, K. E., Kumar, S., Yadava, A., Vahey, M., & Ockenhouse, C. F. (2005) · Infection and Immunity · doi:10.1128/iai.73.9.6091-6100.2005 · Cited by 33
DOCK2 mediates T cell receptor-induced activation of Rac2 and IL-2 transcription
Nishihara, H., Maeda, M., Tsuda, M., Makino, Y., Sawa, H., Nagashima, K., & Tanaka, S. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00931-2 · Cited by 33
Okabe, S., Fukuda, S., & Broxmeyer, H. E. (2002) · Experimental Hematology · doi:10.1016/s0301-472x(02)00823-8 · Cited by 33
García‐Bernal, D., Redondo-Muñóz, J., Dios‐Esponera, A., Chèvre, R., Bailón, E., Garayoa, M., Arellano‐Sánchez, N., Gutierrez, N. C., Hidalgo, A., Garcı́a-Pardo, A., et al. (2012) · The Journal of Pathology · doi:10.1002/path.4066 · Cited by 32
Regulation of mesenchymal‐to‐epithelial transition by PARAXIS during somitogenesis
Rowton, M., Ramos, P., Anderson, D. M., Rhee, J. M., Cunliffe, H. E., & Rawls, A. (2013) · Developmental Dynamics · doi:10.1002/dvdy.24033 · Cited by 34
Silencing of RhoA nucleotide exchange factor, ARHGEF3, reveals its unexpected role in iron uptake
Serbanovic‐Canic, J., Cvejic, A., Soranzo, N., Stemple, D. L., Ouwehand, W. H., & Freson, K. (2011) · Blood · doi:10.1182/blood-2011-02-337295 · Cited by 32
“Immunetworks”, intersecting circuits and dynamics
Jacques Demongeot, A., Elena, A., Noual, M., Sené, S., & Thuderoz, F. (2011) · Journal of Theoretical Biology · doi:10.1016/j.jtbi.2011.03.023 · Cited by 36
Meller, N., Irani-Tehrani, M., Ratnikov, B. I., Paschal, B. M., & Schwartz, M. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404535200 · Cited by 32
Insights from DOCK2 in cell function and pathophysiology
Ji, L., Xu, S., Luo, H., & Zeng, F. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.997659 · Cited by 33
Yasuda, K., Watkins, A. A., Kochar, G. S., Wilson, G. E., Laskow, B., Richez, C., Bonegio, R. G. B., & Rifkin, I. R. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103478 · Cited by 31
Chemoattract Receptor Signaling and Its Role in Lymphocyte Motility and Trafficking
Kehrl, J. H., Hwang, I., & Park, C. (2009) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-93864-4_5 · Cited by 31
Oksanen, A., Aittomäki, S., Jankovic, D. L., Ortutay, Z., Pulkkinen, K. H., Hämäläinen, S., Rokka, A., Corthals, G. L., Watford, W. T., Junttila, I., et al. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1401629 · Cited by 33
DOCK2 regulates cell proliferation through Rac and ERK activation in B cell lymphoma
Wang, L., Nishihara, H., Kimura, T., Kato, Y., Tanino, M. A., Nishio, M., Obara, M., Endo, T., Koike, T., & Tanaka, S. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.03.148 · Cited by 31
Signal Transduction Pathways in Chronic Inflammatory Autoimmune Disease: Small GTPases
Reedquist, K. A., & Tak, P. P. (2012) · The Open Rheumatology Journal · doi:10.2174/1874312901206010259 · Cited by 31
Hara, S., Kiyokawa, E., Iemura, S.-I., Natsume, T., Wassmer, T., Cullen, P. J., Hiai, H., & Matsuda, M. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-03-0314 · Cited by 31
DOCK2 regulates antifungal immunity by regulating RAC GTPase activity
Ma, X., Tan, X., Yu, B., Sun, W., Wang, H., Hu, H., Du, Y., He, R., Gao, R., Peng, Q., et al. (2022) · Cellular and Molecular Immunology · doi:10.1038/s41423-021-00835-0 · Cited by 31
Teng, L., Shen, L., Zhao, W., Wang, C., Feng, S., Wang, Y., Bi, Y., Rong, S., Shushakova, N., Haller, H. G., et al. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.846695 · Cited by 30
Thackray, L. B., Shrestha, B., Richner, J. M., Miner, J. J., Pinto, A. K., Lazear, H. M., Gale, M., & Diamond, M. (2014) · Journal of Virology · doi:10.1128/jvi.01545-14 · Cited by 30
Dimerization of DOCK2 Is Essential for DOCK2-Mediated Rac Activation and Lymphocyte Migration
Terasawa, M., Uruno, T., Mori, S., Kukimoto‐Niino, M., Nishikimi, A., Sanematsu, F., Tanaka, Y., Yokoyama, S., & Fukui, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046277 · Cited by 31
Self-citationJing, Y., Kang, D., Liu, L., Huang, H., Chen, A., Yang, L., Jiang, P., Li, N., Miller, H. E., Liu, Z., et al. (2019) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2019.05.041 · Cited by 30
Cariappa, A., Shoham, T., Liu, H., Levy, S., Boucheix, C., & Pillai, S. S. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.5.2925 · Cited by 30
DOCK2 interacts with FLT3 and modulates the survival of FLT3-expressing leukemia cells
Wu, M. H., Hamaker, M. C., Li, L., Small, D., & Duffield, A. S. (2016) · Leukemia · doi:10.1038/leu.2016.284 · Cited by 29
Manes, T. D., & Pober, J. S. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1201817 · Cited by 28
Novel DOCK2-selective inhibitory peptide that suppresses B-cell line migration
Sakamoto, K., Adachi, Y., Komoike, Y., Kamada, Y., Koyama, R., Fukuda, Y., Kadotani, A., Asami, T., & Sakamoto, J. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.12.170 · Cited by 29
Heterologous regulation of chemokine receptor signaling by the lipid phosphatase SHIP in lymphocytes
Wain, C. M., Westwick, J. K., & Ward, S. G. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2004.12.009 · Cited by 28
DictyosteliumDock180-related RacGEFs Regulate the Actin Cytoskeleton during Cell Motility
Para, A., Krischke, M., Merlot, S., Shen, Z., Oberholzer, M., Lee, S. D., Briggs, S. P., & Firtel, R. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-09-0899 · Cited by 27
IL-23 signaling regulation of pro-inflammatory T-cell migration uncovered by phosphoproteomics
Álvarez-Salamero, C., Castillo‐González, R., Pastor-Fernández, G., Mariblanca, I. R., Pino, J. M. L., Cibrián, D., & Navarro, M. N. (2020) · PLoS Biology · doi:10.1371/journal.pbio.3000646 · Cited by 28
DOCK2 Promotes Pleural Fibrosis by Modulating Mesothelial to Mesenchymal Transition
Qian, G., Adeyanju, O. A., Roy, S., Sunil, C., Jeffers, A., Guo, X., Ikebe, M., Idell, S., & Tucker, T. A. (2021) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2021-0175oc · Cited by 27
Chemokine Signaling to Lymphocyte Integrins Under Shear Flow
Alon, R., & Feigelson, S. W. (2008) · Microcirculation · doi:10.1080/10739680802026076 · Cited by 27
Viau, M., Longo, N. S., Lipsky, P. E., Björck, L., & Zouali, M. (2004) · Infection and Immunity · doi:10.1128/iai.72.6.3515-3523.2004 · Cited by 27
Baker, M. J., Pan, D., & Welch, H. C. E. (2015) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000199 · Cited by 27
Romanova, L. Y., Hashimoto, S., Chay, K.-O., Blagosklonny, M. V., Sabe, H., & Mushinski, J. F. (2004) · Journal of Cell Science · doi:10.1242/jcs.01206 · Cited by 27
Arai, A., Aoki, M., Weihua, Y., Jin, A., & Miura, O. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2006.05.001 · Cited by 27
Park, D., Park, I., Lee, D., Choi, Y. B., Lee, H., & Yun, Y. (2007) · Blood · doi:10.1182/blood-2005-10-061838 · Cited by 27
The regulation of DOCK family proteins on T and B cells
Chen, Y., Chen, Y., Yin, W., Han, H. R., Miller, H. E., Li, J., Herrada, A. A., Kubo, M., Sui, Z., Gong, Q., et al. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.1mr0520-221rr · Cited by 28
Wen, Y., Elliott, M. J., Huang, Y., Miller, T., Corbin, D. R., Hussain, L.-R., Ratajczak, M. Z., Fukui, Y., & Ildstad, S. T. (2014) · Stem Cells · doi:10.1002/stem.1780 · Cited by 26
Self-citationNasreen, M., Ueno, T., Saito, F., & Takahama, Y. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.7.3394 · Cited by 26
The Rac Activator DOCK2 Mediates Plasma Cell Differentiation and IgG Antibody Production
Ushijima, M., Uruno, T., Nishikimi, A., Sanematsu, F., Kamikaseda, Y., Kunimura, K., Sakata, D., Okada, T., & Fukui, Y. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00243 · Cited by 25
Self-citationInsights into the Mechanism for Dictating Polarity in Migrating T-Cells
Niggli, V. (2014) · International review of cytology · doi:10.1016/b978-0-12-800178-3.00007-5 · Cited by 25
Tatsuguchi, T., Uruno, T., Sugiura, Y., Sakata, D., Izumi, Y., Sakurai, T., Hattori, Y., Oki, E., Kubota, N., Nishimoto, K., et al. (2022) · International Immunology · doi:10.1093/intimm/dxac002 · Cited by 25
Self-citationActivation of the immune response is a key feature of aging in mice
Brink, T. C., Regenbrecht, C. R. A., Demetrius, L., Lehrach, H., & Adjaye, J. (2009) · Biogerontology · doi:10.1007/s10522-009-9219-1 · Cited by 24
Microenvironmental Control of High-Speed Interstitial T Cell Migration in the Lymph Node
Katakai, T., & Kinashi, T. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00194 · Cited by 25
The Essential Role of DOCK8 in Humoral Immunity
Randall, K. L., Lambe, T., Goodnow, C. C., & Cornall, R. J. (2010) · Disease Markers · doi:10.1155/2010/143612 · Cited by 24
Reichlin, A., Gazumyan, A., Nagaoka, H., Kirsch, K. H., Kraus, M., Rajewsky, K., & Nussenzweig, M. C. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20031140 · Cited by 24
Addendum: Defective Dock2 expression in a subset of ASC-deficient mouse lines
Ippagunta, S. K., Malireddi, R. K. S., Shaw, P. J., Neale, G. A. M., Walle, L. V., Fukui, Y., Green, D. R., Lamkanfi, M., & Kanneganti, T. (2012) · Nature Immunology · doi:10.1038/ni.2389 · Cited by 23
Self-citationQian, G., Adeyanju, O. A., Sunil, C., Huang, S. K., Chen, S., Tucker, T. A., Idell, S., & Guo, X. (2021) · American Journal Of Pathology · doi:10.1016/j.ajpath.2021.10.011 · Cited by 23
Guenther, C. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.809590 · Cited by 24
Runne, C., & Chen, S. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00879-13 · Cited by 22
Omi, N., Kiyokawa, E., Matsuda, M., Kinoshita, K., Yamada, S., Yamada, K., Matsushima, Y., Wang, Y., Kawai, J., Suzuki, M., et al. (2008) · Experimental Eye Research · doi:10.1016/j.exer.2008.02.011 · Cited by 22
DOCK2 confers immunity and intestinal colonization resistance to Citrobacter rodentium infection
Liu, Z., Man, S. M., Zhu, Q., Vogel, P., Frase, S., Fukui, Y., & Kanneganti, T. (2016) · Scientific Reports · doi:10.1038/srep27814 · Cited by 22
Self-citationGuo, X., Li, F., Xu, Z., Yin, A., Yin, H., Li, C., & Chen, S. (2017) · Journal of Lipid Research · doi:10.1194/jlr.m073049 · Cited by 22
DOCK2 contributes to pulmonary fibrosis by promoting lung fibroblast to myofibroblast transition
Guo, X., Adeyanju, O. A., Sunil, C., Mandlem, V., Olajuyin, A. M., Huang, S. K., Chen, S., Idell, S., Tucker, T. A., & Qian, G. (2022) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00067.2022 · Cited by 21
Worbs, T., & Förster, R. (2009) · Current topics in microbiology and immunology · doi:10.1007/978-3-540-93864-4_4 · Cited by 21
Mechanisms of Tumor Necrosis Factor α Antagonist–Induced Lupus in a Murine Model
Xu, Y., Zhuang, H., Han, S., Liu, C., Wang, H., Mathews, C. E., Massini, J., Yang, L., & Reeves, W. H. (2014) · Arthritis & Rheumatology · doi:10.1002/art.38882 · Cited by 22
Impaired lymphocyte trafficking in mice deficient in the kinase activity of PKN1
Mashud, R., Nomachi, A., Hayakawa, A., Kubouchi, K., Danno, S., Hirata, T., Matsuo, K., Nakayama, T., Satoh, R., Sugiura, R., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-07936-9 · Cited by 21
Self-citationHigh expression of DOCK2 indicates good prognosis in acute myeloid leukemia
Hu, N., Pang, Y., Zhao, H., Si, C., Ding, H., Chen, L., Wang, C., Qin, T., Li, Q., Han, Y., et al. (2019) · Journal of Cancer · doi:10.7150/jca.33244 · Cited by 20
DOCK2 regulates MRGPRX2/B2-mediated mast cell degranulation and drug-induced anaphylaxis
Kunimura, K., Akiyoshi, S., Uruno, T., Matsubara, K., Sakata, D., Morino, K., Hirotani, K., & Fukui, Y. (2023) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2023.01.029 · Cited by 20
Self-citationPodosome regulation by Rho GTPases in myeloid cells
van Helden, S. F. G., & Hordijk, P. L. (2010) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2010.05.008 · Cited by 20
Zhao, H., Adler, K. B., Bai, C., Tang, F., & Wang, X. (2006) · Journal of Proteome Research · doi:10.1021/pr050389v · Cited by 20
Factors governing the intranodal migration behavior of T lymphocytes
Worbs, T., Bernhardt, G., & Förster, R. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00580.x · Cited by 22
Francis, K., Palsson, B. Ø., Donahue, J., Fong, S., & Carrier, E. (2002) · Experimental Hematology · doi:10.1016/s0301-472x(02)00778-6 · Cited by 19
RhoH plays distinct roles in T-cell migrations induced by different doses of SDF1α
Wang, H., Zeng, X. Y., Fan, Z., & Lim, B. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.02.005 · Cited by 19
Attar, M. A., & Santy, L. C. (2013) · BMC Cell Biology · doi:10.1186/1471-2121-14-9 · Cited by 18
Zhang, J., Dong, B., & Siminovitch, K. A. (2009) · Immunological Reviews · doi:10.1111/j.1600-065x.2009.00846.x · Cited by 19
Mehmut, M., Takeda, K., Abe, M., Ogata, H., Hirose, S., Okumura, K., & Fujime, Μ. (2005) · Urologia Internationalis · doi:10.1159/000085934 · Cited by 18
Self-citationInterleukin-8 and other CXC chemokines
Mukaida, N., Ketlinsky, S. A., & Matsushinur, K. (2003) · Elsevier eBooks · doi:10.1016/b978-012689663-3/50050-8 · Cited by 18
DOCK2 Promotes Asthma Development by Eliciting Airway Epithelial–Mesenchymal Transition
Shi, N., Zhang, J., & Chen, S. (2023) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2022-0273oc · Cited by 17
Metadata
- Authors
- Fukui, Y., Hashimoto, O., Sanui, T., Oono, T., Koga, H., Abe, M., Inayoshi, A., Noda, M., Oike, M., Shirai, T., & Sasazuki, T.
- Affiliations
- Kyushu University (JP)
- Kurume University (JP)
- Juntendo University (JP)
- Corresponding author
- Shirai, Toshikazu
- ORCID
- Venue
- Nature
- Published
- 2001-08
- Volume
- 412
- Issue
- 6849
- Pages
- 826-831
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2022157262
- Cited by
- 449
- References
- 30
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 8 · 2023: 14 · 2022: 12 · 2021: 10 · 2020: 9 · 2019: 14 · 2018: 15 · 2017: 18 · 2016: 10 · 2015: 12 · 2014: 23 · 2013: 21 · 2012: 22
- FWCI
- 8.26
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Funders
- University of Michigan
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Health Sciences › Medicine › Oncology › Chemokine receptors and signaling
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Keywords
- DOCK2, lymphocyte chemotaxis, lymphocyte migration, Rac activation, Rho GTPases, actin polymerization, cytoskeletal remodeling, T cells, B cells, marginal zone B cells, lymphopenia, chemokines
- MeSH terms
- Animals, B-Lymphocytes, Carrier Proteins, Cell Line, Chemotaxis, Leukocyte, Cytoskeleton, Female, Hematopoietic Stem Cells, Immunologic Memory, Male, Mice, Inbred C57BL, Spleen, Stem Cells, T-Lymphocytes, Cytokines, Chemokines, CXC, Guanine Nucleotide Exchange Factors, GTPase-Activating Proteins, rac GTP-Binding Proteins, rac1 GTP-Binding Protein, Mice, Chemokine CXCL12
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review