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 301–400 of 448
Dock10 regulates CD23 expression and sustains B-cell lymphopoiesis in secondary lymphoid tissue
García‐Serna, A. M., García, M. J. A., Ruiz-Lafuente, N., Sebastián-Ruiz, S., Martínez, C. M., Moya‐Quiles, M. R., Minguela, A., García-Alonso, A.-M., Martín‐Orozco, E., & Parrado, A. (2016) · Immunobiology · doi:10.1016/j.imbio.2016.07.015 · Cited by 17
Cholesterol sulfate limits neutrophil recruitment and gut inflammation during mucosal injury
Morino, K., Kunimura, K., Sugiura, Y., Izumi, Y., Matsubara, K., Akiyoshi, S., Maeda, R., Hirotani, K., Sakata, D., Mizuno, S., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1131146 · Cited by 17
Self-citationScheikl, T., Reis, B., Pfeffer, K., Holzmann, B., & Beer, S. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.09.023 · Cited by 17
Adhesions ring: A structural comparison between podosomes and the immune synapse
Wernimont, S. A., Cortesio, C. L., Simonson, W. T. N., & Anna Huttenlocher, A. (2008) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2008.01.011 · Cited by 17
Identification of CD36 as a new surface marker of marginal zone B cells by transcriptomic analysis
Zhang, P., Li, W., Wang, Y., Hou, L., Xing, Y., Qin, H., Wang, J., Liang, Y., & Han, H. (2006) · Molecular Immunology · doi:10.1016/j.molimm.2006.02.030 · Cited by 18
Development and Function of B Cell Subsets
Vale, A. M., Kearney, J. F., Nóbrega, A., & Schroeder, H. W. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-397933-9.00007-2 · Cited by 21
Exocrine gland–resident memory CD8 + T cells use mechanosensing for tissue surveillance
Ruef, N., Magdaleno, J. M., Ficht, X., Purvanov, V., Palayret, M., Wissmann, S., Pfenninger, P., Stolp, B., Thelen, F., de Albuquerque, J. B., et al. (2023) · Science Immunology · doi:10.1126/sciimmunol.add5724 · Cited by 16
Li, W., Sun, Y., Yu, L., Chen, R., Gan, R., Qiu, L., Sun, G., Chen, J., Zhou, L., Ding, Y., et al. (2023) · Journal of Clinical Immunology · doi:10.1007/s10875-023-01466-y · Cited by 18
Dock2 participates in bone marrow lympho-hematopoiesis
Kikuchi, T., Kubonishi, S., Shibakura, M., Namba, N., Matsui, T., Fukui, Y., Tanimoto, M., & Katayama, Y. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.12.093 · Cited by 16
Self-citationMolecular Classification of Primary Immunodeficiencies of T Lymphocytes
Comrie, W. A., & Lenardo, M. J. (2018) · Advances in immunology · doi:10.1016/bs.ai.2018.02.003 · Cited by 16
Congenital Defects in Actin Dynamics of Germinal Center B Cells
He, M., & Westerberg, L. S. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00296 · Cited by 17
SHEP1 partners with CasL to promote marginal zone B-cell maturation
Browne, C. D., Hoefer, M. M., Chintalapati, S. K., Cato, M. H., Wallez, Y., Ostertag, D. V., Pasquale, E. B., & Rickert, R. C. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1007558107 · Cited by 16
The Mst1 Kinase Is Required for Follicular B Cell Homing and B-1 B Cell Development
Alsufyani, F., Mattoo, H., Zhou, D., Cariappa, A., Buren, D. V., Hock, H. R., Avruch, J., & Pillai, S. S. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02393 · Cited by 16
B Cell Superantigens Subvert Innate Functions of B Cells
Zouali, M. (2007) · KARGER eBooks · doi:10.1159/000100860 · Cited by 16
PKCθ Regulates T Cell Motility via Ezrin-Radixin-Moesin Localization to the Uropod
Cannon, J. L., Asperti-Boursin, F., Letendre, K. A., Brown, I. K., Korzekwa, K., Blaine, K. M., Oruganti, S. R., Sperling, A. I., & Moses, M. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0078940 · Cited by 16
Stoner, S. A., Liu, K. T. H., Andrews, E. T., Liu, M., Arimoto, K., Yan, M., Davis, A. G., Weng, S., Dow, M. T., Su, X., et al. (2020) · Blood Cancer Journal · doi:10.1038/s41408-020-0282-9 · Cited by 15
Rac signal adaptation controls neutrophil mobilization from the bone marrow
Campa, C. C., Germena, G., Ciraolo, E., Copperi, F., Sapienza, A., Franco, I., Ghigo, A., Camporeale, A., Savino, A. D., Martini, M., et al. (2016) · Science Signaling · doi:10.1126/scisignal.aah5882 · Cited by 14
The role of Dock2 on macrophage migration and functions during Citrobacter rodentium infection
Ji, L., Chen, Y., Xie, L., & Liu, Z. (2021) · Clinical & Experimental Immunology · doi:10.1111/cei.13590 · Cited by 13
Tatsuguchi, T., Uruno, T., Sugiura, Y., Oisaki, K., Takaya, D., Sakata, D., Izumi, Y., Togo, T., Hattori, Y., Kunimura, K., et al. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.04.035 · Cited by 14
Self-citationAdachi, Y., Sakamoto, K., Umemoto, T., Fukuda, Y., Tani, A., & Asami, T. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.02.022 · Cited by 13
Wong, S.-Y., Coffre, M., Ramanan, D., Hines, M. J., Gomez, L. E., Peters, L. A., Schadt, E. E., Koralov, S. B., & Cadwell, K. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1800014 · Cited by 15
Mahajan, V. S., Demissie, E., Alsufyani, F., Kumari, S., Yuen, G. J., Viswanadham, V., Huang, A., Tran, J. Q., Moon, J. J., Irvine, D. J., et al. (2019) · The Journal of Immunology · doi:10.4049/jimmunol.1900440 · Cited by 13
Teng, J., Li, Y., Zhao, Y., Zhang, Y., Chen, D., Liu, J., Cui, M., & Ji, X. S. (2024) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2024.1482901 · Cited by 12
Proteomics Analysis of the Ezrin Interactome in B Cells Reveals a Novel Association with Myo18aα
Matsui, K., Parameswaran, N., Bagheri, N., Willard, B. B., & Gupta, N. (2011) · Journal of Proteome Research · doi:10.1021/pr200577d · Cited by 12
Cao, B., Wang, X., Zhu, L., Zou, R., & Lu, Z. (2019) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2019.01.030 · Cited by 12
Day, C. E., Guillén, C., Willars, G. B., & Wardlaw, A. J. (2010) · Immunology · doi:10.1111/j.1365-2567.2010.03257.x · Cited by 12
Arndt, T., Wedekind, D., Jörns, A., Tsiavaliaris, G., Cuppen, E. P. J. G., Hedrich, H. J., & Lenzen, S. (2015) · Diabetologia · doi:10.1007/s00125-015-3757-7 · Cited by 12
Role of DOCK2 and DOCK180 in fetal thymus colonization
Lei, Y. L., Liu, C., Saito, F., Fukui, Y., & Takahama, Y. (2009) · European Journal of Immunology · doi:10.1002/eji.200939630 · Cited by 12
Self-citationRole of RGS proteins in regulating the migration of B lymphocytes.
Moratz, C. M., Harrison, K., & Kehrl, J. H. (2004) · PubMed · Cited by 12
Machin, P. A., Johnsson, A., Massey, E. J., Pantarelli, C., Chetwynd, S. A., Chu, J. Y., Okkenhaug, H., Segonds-Pichon, A., Walker, S. A., Malliri, A., et al. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1180886 · Cited by 12
Self-citationDOCK8 gene mutation alters cell subsets, BCR signaling, and cell metabolism in B cells
Gu, H., Xie, M., Zhao, S., Luo, X., Huang, Y., Lü, Y., Guan, F., Lei, J., & Liu, C. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07180-w · Cited by 11
Laurin, M., Dumouchel, A., Fukui, Y., & Côté, J. (2013) · Small GTPases · doi:10.4161/sgtp.27430 · Cited by 11
Self-citationT Cell Motility as Modulator of Interactions with Dendritic Cells
Stein, J. V. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00559 · Cited by 11
Kalantari, S., Chashmniam, S., Nafar, M., Samavat, S., Rezaie, D., & Dalili, N. (2020) · OMICS A Journal of Integrative Biology · doi:10.1089/omi.2019.0158 · Cited by 11
Dios‐Esponera, A., de Val, S. I., Sevilla‐Movilla, S., García-Verdugo, R., García‐Bernal, D., Arellano‐Sánchez, N., Cabañas, C., & Teixidó, J. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-07-1246 · Cited by 11
Endothelial PI 3-kinase activity regulates lymphocyte diapedesis
Nakhaei‐Nejad, M., Hussain, A. M., Zhang, Q., & Murray, A. G. (2007) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00321.2007 · Cited by 11
Regulation of focal adhesion and cell migration by ANKRD28-DOCK180 interaction
Kiyokawa, E., & Matsuda, M. (2009) · Cell Adhesion & Migration · doi:10.4161/cam.3.3.8857 · Cited by 11
Review: Tissue Engineering Technology to Enhance Cell Recruitment for Regeneration Therapy
Kohara, H., & Tabata, Y. (2010) · Institutional Repositories DataBase (IRDB) · Cited by 11
DOCK2 Promotes Atherosclerosis by Mediating the Endothelial Cell Inflammatory Response
Qian, G., Adeyanju, O. A., Cai, D., Tucker, T. A., Idell, S., Chen, S., & Guo, X. (2023) · American Journal Of Pathology · doi:10.1016/j.ajpath.2023.09.015 · Cited by 10
Fernández-Calleja, V., Hernández, P., Schvartzman, J. B., de Lacoba, M. G., & Krimer, D. B. (2017) · PeerJ · doi:10.7717/peerj.3432 · Cited by 11
GPCRs that Rhoar the Guanine nucleotide exchange factors
Omble, A., & Kulkarni, K. A. (2021) · Small GTPases · doi:10.1080/21541248.2021.1896963 · Cited by 10
Rap1 organizes lymphocyte front-back polarity via RhoA signaling and talin1
Ueda, Y., Higasa, K., Kamioka, Y., Kondo, N., Horitani, S., Ikeda, Y., Bergmeier, W., Fukui, Y., & Kinashi, T. (2023) · iScience · doi:10.1016/j.isci.2023.107292 · Cited by 10
Self-citationWang, D., Ling, J., Tan, R., Wang, H., Qu, Y., Li, X., Lin, J. E., Zhang, Q., Hu, Q., Liu, Z., et al. (2024) · iScience · doi:10.1016/j.isci.2024.109213 · Cited by 9
Hwang, I., Kim, J. S., Harrison, K. A., Park, C., Shi, C. S., & Kehrl, J. H. (2024) · Science Signaling · doi:10.1126/scisignal.ade1119 · Cited by 10
A Phosphoproteomic Analysis of Mycobacterial PknG-Mediated Host Immune Evasion
Baros‐Steyl, S. S., Nakedi, K. C., Ganief, T. A., Okendo, J., Tabb, D., Soares, N. C., & Blackburn, J. M. (2025) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5c00416 · Cited by 9
An Emerging Role for PI5P in T Cell Biology
Nunès, J. A., & Guittard, G. C. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00080 · Cited by 9
Rac and cell migration: CDM proteins integrate signals
Bourne, H. R. (2005) · Nature Cell Biology · doi:10.1038/ncb0805-777 · Cited by 9
Molecular and Cellular Mechanisms Associated with Autoimmune Diseases
Ayensu, W. K., Tchounwou, P. B., & McMurray, R. W. (2004) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph2004010039 · Cited by 9
Immunoactinopathies revisited: understanding clinical manifestations and biological pathways
Hiensch, F., Dupré, L., & Salzer, E. (2025) · Blood · doi:10.1182/blood.2024026763 · Cited by 9
Randall, K. L., Flesch, I. E. A., Mei, Y., Miosge, L. A., Aye, R., Yu, Z., Domaschenz, H., Hollett, N. A., Russell, T., Stefanovic, T., et al. (2024) · The Journal of Infectious Diseases · doi:10.1093/infdis/jiae077 · Cited by 8
Rho and Rap guanosine triphosphatase signaling in B cells and chronic lymphocytic leukemia
Mele, S., Devereux, S., & Ridley, A. J. (2013) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2013.866666 · Cited by 8
Extra-hematopoietic immunomodulatory role of the guanine-exchange factor DOCK2
Scharler, C., Poupardin, R., Peking, P., Wolf, M., Schreck, C., Brachtl, G., Andrade, A. C., Krisch, L. M., Daheron, L. M., Schallmoser, K., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-04078-1 · Cited by 8
Antibody Binding to CD4 Induces Rac GTPase Activation and Alters T Cell Migration
Morillon, Y. M., Lessey-Morillon, E. C., Clark, M., Zhang, R., Wang, B., Burridge, K., & Tisch, R. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501600 · Cited by 8
Miao, S., Zhang, R., Wang, W. T., Wang, H., Meng, L., Zu, L., & Fu, G. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.27151 · Cited by 8
Trushin, S. A., Bren, G. D., & Badley, A. D. (2010) · The Open Virology Journal · doi:10.2174/1874357901004010157 · Cited by 8
Ji, J., Xu, X., Zhang, L., Liu, S., Chen, J., Gao, H., Xiang, L., Li, Y., Xu, H., Chen, Y., et al. (2025) · Cardiovascular Research · doi:10.1093/cvr/cvaf009 · Cited by 7
The Tec Kinase Itk Integrates Naïve T Cell Migration and In Vivo Homeostasis
Thelen, F., Wissmann, S., Ruef, N., & Stein, J. V. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.716405 · Cited by 7
DOCK2 Mutation and Recurrent Hemophagocytic Lymphohistiocytosis
Reiff, D. D., Zhang, M., & Cron, R. Q. (2023) · Life · doi:10.3390/life13020434 · Cited by 7
DOCK2 Deficiency Attenuates Abdominal Aortic Aneurysm Formation—Brief Report
Guo, X., Cai, D., Dong, K., Li, C., Xu, Z., & Chen, S. (2023) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.122.318400 · Cited by 7
Regulation of global CD8+ T‐cell positioning by the actomyosin cytoskeleton
Stein, J. V., & Ruef, N. (2019) · Immunological Reviews · doi:10.1111/imr.12759 · Cited by 7
Kim, S. J., Park, S. E., Jeong, J. B., Oh, S. J., Choi, A., Kim, Y. H., Choi, S., Oh, S., Ryu, G. H., Jeon, H. B., et al. (2022) · Stem Cells International · doi:10.1155/2022/4711499 · Cited by 7
Das, N. D., Jung, K. H., Park, J. H., Choi, M., Lee, H. T., Kim, M. S., Lee, S. R., & Chai, Y. G. (2012) · Journal of Medicinal Food · doi:10.1089/jmf.2011.1998 · Cited by 6
The Proline-Rich Region of HIV-1 Nef Affects CXCR4-Mediated Chemotaxis in Jurkat T Cells
Lee, C. M. Y., Gala, S., Stewart, G. J., & Williamson, P. (2008) · Viral Immunology · doi:10.1089/vim.2007.0093 · Cited by 6
Interplay of Polarity Proteins and GTPases in T-Lymphocyte Function
Fung, I. T. H., Russell, S. M., & Oliaro, J. (2012) · Clinical and Developmental Immunology · doi:10.1155/2012/417485 · Cited by 6
Wissmann, S., Stolp, B., Marcos‐Jiménez, A., & Stein, J. V. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.982383 · Cited by 5
Yamamoto, Y., Shirai, Y., Edahiro, R., Kumanogoh, A., & Okada, Y. (2024) · Immunological Medicine · doi:10.1080/25785826.2024.2394258 · Cited by 5
Starfish ApDOCK protein essentially functions in larval defense system operated by mesenchyme cells
Furukawa, R., Funabashi, H., Matsumoto, M., & Kaneko, H. (2012) · Immunology and Cell Biology · doi:10.1038/icb.2012.37 · Cited by 5
Suo, D., Liang, L., Xia, Z., Zhang, Y., Zeng, T., Li, S., Guan, X., & Li, Y. (2025) · Cellular Oncology · doi:10.1007/s13402-025-01090-5 · Cited by 4
Jia, Y., Sun, J., Chen, S., Bian, Y., Jiang, A., Liang, H., & Du, X. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2024.119894 · Cited by 4
Immunological Synapse Formation: Cell Polarity During T Cell–APC Interaction
Liu, X., & Huse, M. (2015) · Springer eBooks · doi:10.1007/978-3-319-14463-4_11 · Cited by 4
Human Mesenchymal Stem Cells Migrate toward Colon Cancer Partially Regulated by HMGB1
ホシノ, ゴ. (2013) · Journal of Cell Science & Therapy · doi:10.4172/2157-7013.1000145 · Cited by 4
Modulation of Monomeric G Proteins by Phosphoinositides
Vermeren, S., Stephens, L., & Hawkins, P. T. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00140-6 · Cited by 4
Chen, Y., Di, M., Tang, Y., & Xia, J. (2021) · Annals of Blood · doi:10.21037/aob-21-5 · Cited by 4
Development and Function of B Cell Subsets
Kearney, J. F. (2004) · Elsevier eBooks · doi:10.1016/b978-012053641-2/50011-3 · Cited by 4
Chemokines in Cell Movement and Allergic Inflammation
Mikhak, Z., & Luster, A. D. (2009) · Elsevier eBooks · doi:10.1016/b978-0-323-05659-5.00011-5 · Cited by 4
Dynamics of B Cell Migration to and within Secondary Lymphoid Organs
Cyster, J. G., & von Andrian, U. H. (2004) · Elsevier eBooks · doi:10.1016/b978-012053641-2/50015-0 · Cited by 4
Neel, N. F. (2008) · Europe PMC (PubMed Central) · Cited by 4
Li, X., Shen, W., Chen, J., Lv, H., He, W., He, T., Guo, T., & Liu, Z. (2025) · Molecular Immunology · doi:10.1016/j.molimm.2025.03.004 · Cited by 3
DOCK2 as a novel CD11c ligand in neutrophils to regulate reactive oxygen species production
Koutsogiannaki, S., Hou, L., Alhamdan, F., Mastali, M., Murray, C., Eyk, J. E. V., Kunimura, K., & Yuki, K. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1692451 · Cited by 3
T-lymphocyte navigation and migration: beyond the PI3K paradigm
Smith, L., Webb, A., & Ward, S. G. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350193 · Cited by 3
Hu, B., Symons, M. H., Salhia, B., Ensign, S. P. F., Tran, N. L., Rutka, J. T., & Cheng, S. (2011) · Springer eBooks · doi:10.1007/978-94-007-2558-4_6 · Cited by 3
Peters, D. E., Norris, L., & Slusher, B. S. (2019) · Crohn s & Colitis 360 · doi:10.1093/crocol/otz030 · Cited by 3
Polar Cell Growth and the Cytoskeleton Biology
Hussey, P. J., Deeks, M. J., Hawkins, T. J., & Ketelaar, T. (2017) · Wiley eBooks · doi:10.1002/9781119312994.apr0110 · Cited by 3
Pan, Y., Sun, Y., Xiao, Y., Ding, J., Hu, G., Lin, Z., & Chen, C. (2025) · Clinical and Experimental Medicine · doi:10.1007/s10238-025-01653-8 · Cited by 2
Rho Family GTPases and their Modulators
Lin, Y., & Zheng, Y. (2023) · Springer eBooks · doi:10.1007/978-3-031-23752-2_18 · Cited by 3
Activation of GTPases by Dock180 Family of Proteins
Lu, M., & Ravichandran, K. S. (2005) · Springer eBooks · doi:10.1007/1-4020-3462-8_4 · Cited by 2
Buckland, J. (2001) · Nature reviews. Immunology · doi:10.1038/35095531 · Cited by 2
Cui, H., & Liu, G. (2021) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2021-0411ed · Cited by 2
DOCK2 protects against bacterial sepsis by constraining T helper 1 response
Ye, S., Huang, L., Zheng, Y., Liu, S., Wang, X., Yu, H., Zhu, L., Liang, T., Wang, Y., Zhang, C., et al. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1527934 · Cited by 1
The TCR-SUB1-DOCK2 axis promotes autoimmunity by driving pathogenic CD4+ T cell tissue infiltration
Li, X.-X., Liang, W., Wang, W., Sherman, E., Huang, K., & Wang, F. (2025) · Immunity · doi:10.1016/j.immuni.2025.11.009 · Cited by 1
DOCK2 in Disease: Emerging Insights and Research Advances
Yu, Z., Jin, S., Wan, S., Zhang, Z., Jiang, Y., Li, J., & Wu, S. (2025) · Immunological Investigations · doi:10.1080/08820139.2025.2596074 · Cited by 1
Lymphoid tissue chemokines limit priming duration to preserve CD8 + T cell functionality
Altenburger, L. M., Carvoeiro, D. C., Dehio, P., Zhou, J., Laura, C., Cuadros, À. B. I., Katoch, M., Krüger, C., de Albuquerque, J. B., Pfenninger, P., et al. (2026) · Science · doi:10.1126/science.adq2080 · Cited by 1
Basic Rules of T Cell Migration
Stein, J. V., Moalli, F., & Ackerknecht, M. (2016) · Resistance to targeted anti-cancer therapeutics · doi:10.1007/978-3-319-42223-7_1 · Cited by 1
Cholesterol sulfate prevents maternal-fetal conflict by locally modulating immune reactivity
Hirotani, K., Kunimura, K., Maeda, R., Sugiura, Y., Nakata, K., Takahashi, M., Izumi, Y., Akiyoshi, S., Matsubara, K., Morino, K., et al. (2025) · Placenta · doi:10.1016/j.placenta.2025.07.034 · Cited by 1
Self-citationIntracellular signaling pathways mediating lymphocyte trafficking
Nombela‐Arrieta, C. (2008) · Inmunología · doi:10.1016/s0213-9626(08)70067-2 · Cited by 1
Steele, A. J. (2018) · Blood · doi:10.1182/blood-2018-05-848382 · Cited by 1
Kusumoto, T., Chubachi, S., Namkoong, H., Tanaka, H., Lee, H., Otake, S., Nakagawara, K., Fukushima, T., Morita, A., Watase, M., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-49340-6 · Cited by 1
EFFECTOR T CELL HOMING TO THE SMALL INTESTINAL MUCOSA
Stenstad, H. (2007) · Lund University Publications (Lund University) · Cited by 1
Hamel, B. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/kmq6-qg97 · Cited by 1
(2009) · Chemical industries · doi:10.1201/9781420059656-p8 · Cited by 1
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