Cited by 354Barrier Structure and Function StudiesProtein Kinase Regulation and GTPase SignalingCell Adhesion Molecules Research

The DOI matches its Crossref record; 57 of the 58 references it cites were found in a registry or an index.

Structural and Functional Regulation of Tight Junctions by RhoA and Rac1 Small GTPases

Open access

Jou, Tzuu-Shuh, Schneeberger, Eveline E., James Nelson, W.·1998·The Journal of Cell Biology

DOI 10.1083/jcb.142.1.101PMC PMC2133025

Open this paper in CoChat — free account

Abstract

Tight junctions (TJ) govern ion and solute diffusion through the paracellular space (gate function), and restrict mixing of membrane proteins and lipids between membrane domains (fence function) of polarized epithelial cells. We examined roles of the RhoA and Rac1 GTPases in regulating TJ structure and function in MDCK cells using the tetracycline repressible transactivator to regulate RhoAV14, RhoAN19, Rac1V12, and Rac1N17 expression. Both constitutively active and dominant negative RhoA or Rac1 perturbed TJ gate function (transepithelial electrical resistance, tracer diffusion) in a dose-dependent and reversible manner. Freeze-fracture EM and immunofluoresence microscopy revealed abnormal TJ strand morphology and protein (occludin, ZO-1) localization in RhoAV14 and Rac1V12 cells. However, TJ strand morphology and protein localization appeared normal in RhoAN19 and Rac1N17 cells. All mutant GTPases disrupted the fence function of the TJ (interdomain diffusion of a fluorescent lipid), but targeting and organization of a membrane protein in the apical membrane were unaffected. Expression levels and protein complexes of occludin and ZO-1 appeared normal in all mutant cells, although ZO-1 was more readily solubilized from RhoAV14-expressing cells with Triton X-100. These results show that RhoA and Rac1 regulate gate and fence functions of the TJ, and play a role in the spatial organization of TJ proteins at the apex of the lateral membrane.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1083/jcb.142.1.101

Cites

57 of 57 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Rho GTPases and the Actin Cytoskeleton
Hall, A. (1998) · Science · doi:10.1126/science.279.5350.509 · Cited by 6,138
Tight control of gene expression in mammalian cells by tetracycline-responsive promoters.
Gossen, M., & Bujard, H. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5547 · Cited by 4,943 · cited 1×
“To study roles of RhoA and Rac1 in the structural and functional organization of TJ, we generated MDCK cells that express RhoA and Rac1 mutants under the control of the tetracycline repressible transactivator (Gossen and Bujard, 1992).”
Background
The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
Ridley, A. J., & Hall, A. (1992) · Cell · doi:10.1016/0092-8674(92)90163-7 · Cited by 4,469
JUNCTIONAL COMPLEXES IN VARIOUS EPITHELIA
Farquhar, M. G., & Palade, G. E. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.17.2.375 · Cited by 3,637
The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D., & Hall, A. (1992) · Cell · doi:10.1016/0092-8674(92)90164-8 · Cited by 3,616
Regulation of Myosin Phosphatase by Rho and Rho-Associated Kinase (Rho-Kinase)
Kimura, K., Ito, M., Amano, M., Chihara, K., Fukata, Y., Nakafuku, M., Yamamori, B., Feng, J., Nakano, T., Okawa, K., et al. (1996) · Science · doi:10.1126/science.273.5272.245 · Cited by 2,889
Occludin: a novel integral membrane protein localizing at tight junctions.
Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., Tsukita, S., & Tsukita, S. (1993) · The Journal of cell biology · doi:10.1083/jcb.123.6.1777 · Cited by 2,580
Phosphorylation and Activation of Myosin by Rho-associated Kinase (Rho-kinase)
Amano, M., Ito, M., Kimura, K., Fukata, Y., Chihara, K., Nakano, T., Matsuura, Y., & Kaibuchi, K. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.34.20246 · Cited by 2,009
Proteins regulating Ras and its relatives
Boguski, M. S., & McCormick, F. P. (1993) · Nature · doi:10.1038/366643a0 · Cited by 1,905
Recognition of Unique Carboxyl-Terminal Motifs by Distinct PDZ Domains
Songyang, Z., Fanning, A. S., Fu, C., Xu, J., Marfatia, S. M., Chishti, A. H., Crompton, A., Chan, A. C., Anderson, J. M., & Cantley, L. C. (1997) · Science · doi:10.1126/science.275.5296.73 · Cited by 1,385

Flagged first, then by citations

Show all 58 references

1 of the 58 references couldn’t be matched to a known paper.

Sorted by citations

Intestinal mucosal barrier function in health and disease
Turner, J. R. (2009) · Nature reviews. Immunology · doi:10.1038/nri2653 · Cited by 3,952
Multifunctional strands in tight junctions
Tsukita, S., Furuse, M., & Itoh, M. (2001) · Nature reviews. Molecular cell biology · doi:10.1038/35067088 · Cited by 2,578
Cancer-secreted miR-105 destroys vascular endothelial barriers to promote metastasis
Zhou, W., Fong, M. Y., Min, Y., Somlo, G., Liu, L., Palomares, M. R., Yu, Y., Chow, A., O’Connor, S. T. F., Chin, A. R., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.03.007 · Cited by 1,476
The Tight Junction Protein ZO-1 Establishes a Link between the Transmembrane Protein Occludin and the Actin Cytoskeleton
Fanning, A. S., Jameson, B. J., Jesaitis, L. A., & Anderson, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.45.29745 · Cited by 1,432
The tight junction: a multifunctional complex.
Schneeberger, E., & Lynch, R. D. (2004) · American Journal of Physiology - Cell Physiology · doi:10.1152/ajpcell.00558.2003 · Cited by 1,450
Self-citation
Endothelial Cell-to-Cell Junctions: Molecular Organization and Role in Vascular Homeostasis
Bazzoni, G., & Dejana, E. (2004) · Physiological Reviews · doi:10.1152/physrev.00035.2003 · Cited by 1,384
Tight junctions of the blood-brain barrier: development, composition and regulation.
Wolburg, H., & Lippoldt, A. (2002) · PubMed · doi:10.1016/s1537-1891(02)00200-8 · Cited by 1,236
Regulation of the Cytoskeleton and Cell Adhesion by the Rho Family GTPases in Mammalian Cells
Kaibuchi, K., Kuroda, S., & Amano, M. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.459 · Cited by 1,017
Proinflammatory Cytokines Disrupt Epithelial Barrier Function by Apoptosis-Independent Mechanisms
Bruewer, M., Luegering, A., Kucharzik, T. F., Parkos, C. A., Madara, J., Hopkins, A. M., & Nusrat, A. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.11.6164 · Cited by 897
Signalling to and from tight junctions
Matter, K., & Balda, M. (2003) · Nature reviews. Molecular cell biology · doi:10.1038/nrm1055 · Cited by 926
Crosstalk of tight junction components with signaling pathways
González-Mariscal, L., Tapia, R., & Chamorro, D. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.08.018 · Cited by 759
A mammalian PAR-3–PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
Lin, D., Edwards, A. S., Fawcett, J. P., Mbamalu, G., Scott, J. D., & Pawson, T. (2000) · Nature Cell Biology · doi:10.1038/35019582 · Cited by 743
The Blood-Brain Barrier in Brain Homeostasis and Neurological Diseases
Weiss, N., Miller, F., Cazaubon, S., & Couraud, P.-O. (2009) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.10.022 · Cited by 731
Localization of apical epithelial determinants by the basolateral PDZ protein Scribble
Bilder, D., & Perrimon, N. (2000) · Nature · doi:10.1038/35001108 · Cited by 716
Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10
Chiang, S.-H., Baumann, C. A., Kanzaki, M., Thurmond, D. C., Watson, R. T., Neudauer, C. L., Macara, I. G., Pessin, J. E., & Saltiel, A. R. (2001) · Nature · doi:10.1038/35073608 · Cited by 611
Cell junction dynamics in the testis: Sertoli-germ cell interactions and male contraceptive development.
Cheng, Y. C., & Mruk, D. (2002) · Physiological Reviews · doi:10.1152/physrev.00009.2002 · Cited by 631
Regulation of tight junctions and loss of barrier function in pathophysiology.
Harhaj, N. S., & Antonetti, D. (2004) · International Journal of Biochemistry and Cell Biology · doi:10.1016/j.biocel.2003.08.007 · Cited by 573
Tight Junctions of the Blood–Brain Barrier
Kniesel, U., & Wolburg, H. (2000) · Cellular and Molecular Neurobiology · doi:10.1023/a:1006995910836 · Cited by 535
E‐cadherin is essential for in vivo epidermal barrier function by regulating tight junctions
Tunggal, J. A., Helfrich, I., Schmitz, A., Schwarz, H., Günzel, D., Fromm, M., Kemler, R., Krieg, T., & Niessen, C. M. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600605 · Cited by 491
Occludin: Structure, function and regulation
FELDMAN, G., Mullin, J. M., & RYAN, M. (2005) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2005.01.009 · Cited by 512
ZO-1 Stabilizes the Tight Junction Solute Barrier through Coupling to the Perijunctional Cytoskeleton
Itallie, C. M. V., Fanning, A. S., Bridges, A. S., & Anderson, J. M. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-04-0320 · Cited by 479
Rac1 orientates epithelial apical polarity through effects on basolateral laminin assembly
O’Brien, L. E., Jou, T., Pollack, A. L., Zhang, Q., Hansen, S. H., Yurchenco, P. D., & Mostov, K. E. (2001) · Nature Cell Biology · doi:10.1038/ncb0901-831 · Cited by 485
Self-citation
Myosin light chain phosphorylation regulates barrier function by remodeling tight junction structure
Shen, L., Black, E. D., Witkowski, E. D., Lencer, W. I., Guerriero, V., Schneeberger, E. E., & Turner, J. R. (2006) · Journal of Cell Science · doi:10.1242/jcs.02915 · Cited by 467
Self-citation
Rho and Rac but not Cdc42 regulate endothelial cell permeability
Wójciak‐Stothard, B., Potempa, S., Eichholtz, T. J., & Ridley, A. J. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.7.1343 · Cited by 465
Epithelial myosin light chain kinase-dependent barrier dysfunction mediates T cell activation-induced diarrhea in vivo
Clayburgh, D. R. (2005) · Journal of Clinical Investigation · doi:10.1172/jci24970 · Cited by 419
Myosin Vb Is Associated with Plasma Membrane Recycling Systems
Lapierre, L. A., Kumar, R., Hales, C. M., Navarre, J., Bhartur, S. G., Burnette, J. O., Provance, D. W., Mercer, J. A., Bähler, M., & Goldenring, J. R. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.6.1843 · Cited by 424
Cortactin Localization to Sites of Actin Assembly in Lamellipodia Requires Interactions with F-Actin and the Arp2/3 Complex
Weed, S. A., Karginov, A. V., Schafer, D. A., Weaver, A. M., Kinley, A. W., Cooper, J. A., & Parsons, J. T. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.1.29 · Cited by 423
Dynamics and functions of tight junctions
Steed, E., Balda, M. S., & Matter, K. (2010) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.12.002 · Cited by 418
A Rich1/Amot complex regulates the Cdc42 GTPase and apical-polarity proteins in epithelial cells.
Wells, C., Fawcett, J. P., Traweger, A., Yamanaka, Y., Goudreault, M., Elder, K. D., Kulkarni, S. V., Gish, G., Virag, C., Lim, C. S. H., et al. (2006) · Cell · doi:10.1016/j.cell.2006.02.045 · Cited by 407
β1-Integrin Orients Epithelial Polarity via Rac1 and Laminin
Yu, W., Datta, A., Leroy, P., O’Brien, L. E., Mak, G. Z., Jou, T., Matlin, K. S., Mostov, K. E., & Zegers, M. M. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-05-0435 · Cited by 375
Self-citation
Spatio-Temporal Regulation of Rac1 Localization and Lamellipodia Dynamics during Epithelial Cell-Cell Adhesion
Ehrlich, J. S., Hansen, M. D. H., & Nelson, W. J. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00216-2 · Cited by 358
Clostridium difficile Toxins Disrupt Epithelial Barrier Function by Altering Membrane Microdomain Localization of Tight Junction Proteins
Nusrat, A., von Eichel-Streiber, C., Turner, J. R., Verkade, P., Madara, J., & Parkos, C. A. (2001) · Infection and Immunity · doi:10.1128/iai.69.3.1329-1336.2001 · Cited by 352
Actin Cable Dynamics and Rho/Rock Orchestrate a Polarized Cytoskeletal Architecture in the Early Steps of Assembling a Stratified Epithelium
Vaezi, A., Bauer, C., Vasioukhin, V., & Fuchs, E. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00259-9 · Cited by 349
Reactive oxygen species alter brain endothelial tight junction dynamics via RhoA, PI3 kinase and PKB signaling
Schreibelt, G., Kooij, G., Reijerkerk, A., van Doorn, R., Gringhuis, S. I., van der Pol, S., Weksler, B. B., Romero, I. A., Couraud, P., Piontek, J., et al. (2007) · The FASEB Journal · doi:10.1096/fj.07-8329com · Cited by 347
Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
Kroschewski, R., Hall, A., & Mellman, I. (1999) · Nature Cell Biology · doi:10.1038/8977 · Cited by 344
Cell–cell adhesion and signalling
Braga, V. M. M. (2002) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00373-3 · Cited by 328
The transcription factor Snail downregulates the tight junction components independently of E-cadherin downregulation
Ohkubo, T., & Ozawa, M. (2004) · Journal of Cell Science · doi:10.1242/jcs.01004 · Cited by 322
Tight junctions: molecular architecture and function.
Aijaz, S., Balda, M., & Matter, K. (2006) · International Review of Cytology · doi:10.1016/s0074-7696(06)48005-0 · Cited by 325
Nonsteroidal Anti-Inflammatory Drugs Can Lower Amyloidogenic Aß 42 by Inhibiting Rho
Zhou, Y., Su, Y., Li, B., Liu, F., Ryder, J. W., Wu, X., Gonzalez-DeWhitt, P. A., Gelfanova, V., Hale, J. E., May, P. C., et al. (2003) · Science · doi:10.1126/science.1090154 · Cited by 316
Regulation of Tight Junction Permeability and Occludin Phosphorylation by RhoA-p160ROCK-dependent and -independent Mechanisms
Hirase, T., Kawashima, S., Wong, E. Y. M., Ueyama, T., Rikitake, Y., Tsukita, S., Yokoyama, M., & Staddon, J. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007136200 · Cited by 312
Cingulin Contains Globular and Coiled-Coil Domains and Interacts with Zo-1, Zo-2, Zo-3, and Myosin
Cordenonsi, M., D’Atri, F., Hammar, E. B., Parry, D. A. D., Kendrick‐Jones, J., Shore, D., & Citi, S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.147.7.1569 · Cited by 319
Transmembrane proteins in the tight junction barrier
FANNING, A. S., MITIC, L. L., & ANDERSON, J. M. (1999) · Journal of the American Society of Nephrology · doi:10.1681/asn.v1061337 · Cited by 301
Endothelial tight junctions and their regulatory signaling pathways in vascular homeostasis and disease
Cong, X., & Kong, W. (2019) · Cellular Signalling · doi:10.1016/j.cellsig.2019.109485 · Cited by 312
Septins and the Lateral Compartmentalization of Eukaryotic Membranes
Caudron, F., & Barral, Y. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.04.003 · Cited by 296
Effects of Regulated Expression of Mutant RhoA and Rac1 Small GTPases on the Development of Epithelial (MDCK) Cell Polarity
Jou, T., & Nelson, W. J. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.1.85 · Cited by 290
Self-citation
The digestive neuronal–glial–epithelial unit: a new actor in gut health and disease
Neunlist, M., Landeghem, L. V., Mahé, M. M., Derkinderen, P., Varannes, S. B. D., & Rolli‐Derkinderen, M. (2012) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2012.221 · Cited by 277
A human homolog of the C. elegans polarity determinant Par-6 links Rac and Cdc42 to PKCζ signaling and cell transformation
Qiu, R., Abo, A., & Martin, G. S. (2000) · Current Biology · doi:10.1016/s0960-9822(00)00535-2 · Cited by 275
Adenosine Receptor Signaling Modulates Permeability of the Blood–Brain Barrier
Carman, A. J., Mills, J. H., Krenz, A., Kim, D.-G., & Bynoe, M. S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.3337-11.2011 · Cited by 276
Restoration of Tight Junction Structure and Barrier Function by Down-Regulation of the Mitogen-activated Protein Kinase Pathway in Ras-transformed Madin-Darby Canine Kidney Cells
Chen, Y., Lu, Q., Schneeberger, E. E., & Goodenough, D. A. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.3.849 · Cited by 274
Self-citation
Inflammatory pain alters blood-brain barrier permeability and tight junctional protein expression
Huber, J. D., Witt, K. A., Hom, S., Egleton, R. D., Mark, K. S., & Davis, T. P. (2001) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.2001.280.3.h1241 · Cited by 266
Functional analysis of tight junctions
Matter, K., & Balda, M. S. (2003) · Methods · doi:10.1016/s1046-2023(03)00029-x · Cited by 265
Molecular basis of endothelial cell morphogenesis in three‐dimensional extracellular matrices
Davis, G. E., Bayless, K. J., & Mavila, A. (2002) · The Anatomical Record · doi:10.1002/ar.10159 · Cited by 247
Cloning of a novel human Rac1b splice variant with increased expression in colorectal tumors
Jordan, P., BrazÃ£o, R., Boavida, M. G., Gespach, C. P., & Chastre, E. (1999) · Oncogene · doi:10.1038/sj.onc.1203233 · Cited by 261
Bacterial cytotoxins: targeting eukaryotic switches
Aktories, K., & Barbieri, J. T. (2005) · Nature Reviews Microbiology · doi:10.1038/nrmicro1150 · Cited by 261
Par6–aPKC uncouples ErbB2 induced disruption of polarized epithelial organization from proliferation control
Aranda, V., Haire, T., Nolan, M. E., Calarco, J. P., Rosenberg, A. Z., Fawcett, J. P., Pawson, T. J., & Muthuswamy, S. K. (2006) · Nature Cell Biology · doi:10.1038/ncb1485 · Cited by 247
“You Shall Not Pass”—tight junctions of the blood brain barrier
Bauer, H., Krizbai, I. A., Bauer, H., & Traweger, A. (2014) · Frontiers in Neuroscience · doi:10.3389/fnins.2014.00392 · Cited by 255
From Mechanical Force to RhoA Activation
Lessey, E. C., Guilluy, C., & Burridge, K. (2012) · Biochemistry · doi:10.1021/bi300758e · Cited by 247
The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex
Mertens, A. E. E., Rygiel, T. P., Olivo, C., van der Kammen, R., & Collard, J. G. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200502129 · Cited by 238
Role of Rho family GTPases in epithelial morphogenesis.Preprint
Aelst, L. V., & Symons, M. (2002) · Genes & Development · doi:10.1101/gad.978802 · Cited by 247
Rho family GTPases: more than simple switches
Symons, M. H., & Settleman, J. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01832-8 · Cited by 236
HIF-dependent regulation of claudin-1 is central to intestinal epithelial tight junction integrity
Saeedi, B. J., Kao, D. J., Kitzenberg, D., Dobrinskikh, E., Schwisow, K. D., Masterson, J. C., Kendrick, A. A., Kelly, C. J., Bayless, A. J., Kominsky, D. J., et al. (2015) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-07-1194 · Cited by 235
Oncogenic Raf-1 Disrupts Epithelial Tight Junctions via Downregulation of Occludin
Li, D., & Mrsny, R. J. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.4.791 · Cited by 233
RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin
Bruewer, M., Hopkins, A. M., Hobert, M. E., Nusrat, A., & Madara, J. (2004) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00087.2004 · Cited by 223
Rho kinase regulates tight junction function and is necessary for tight junction assembly in polarized intestinal epithelia
Walsh, S. V., Hopkins, A. M., Chen, J. Z., Narumiya, S., Parkos, C. A., & Nusrat, A. (2001) · Gastroenterology · doi:10.1053/gast.2001.27060 · Cited by 211
The cytoplasmic plaque of tight junctions: a scaffolding and signalling center.
Guillemot, L., Paschoud, S., Pulimeno, P., Foglia, A., & Citi, S. (2008) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamem.2007.09.032 · Cited by 207
Identification of a tight junction–associated guanine nucleotide exchange factor that activates Rho and regulates paracellular permeability
Benais-Pont, G., Punn, A., Flores-Maldonado, C., Eckert, J. J., Raposo, G., Fleming, T. P., Cereijido, M., Balda, M. S., & Matter, K. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211047 · Cited by 202
Constitutive activation of Rho proteins by CNF-1 influences tight junction structure and epithelial barrier function
Hopkins, A. M., Walsh, S. V., Verkade, P., Boquet, P., & Nusrat, A. (2003) · Journal of Cell Science · doi:10.1242/jcs.00300 · Cited by 202
Epithelial junctions and Rho family GTPases: the zonular signalosome
Citi, S., Guerrera, D., Spadaro, D., & Shah, J. (2014) · Small GTPases · doi:10.4161/21541248.2014.973760 · Cited by 211
Na,K-ATPase Activity Is Required for Formation of Tight Junctions, Desmosomes, and Induction of Polarity in Epithelial Cells
Langhans, S. A., Palmer, L. G., Moon, S. Y., Soler, A. P., Apodaca, G. L., Harper, J. F., Zheng, Y., & Rajasekaran, A. K. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.12.3717 · Cited by 192
The role of Rho GTPases in disease development
Boettner, B., & Van Aelst, L. (2002) · Gene · doi:10.1016/s0378-1119(02)00426-2 · Cited by 229
Cadherins in collective cell migration of mesenchymal cells
Théveneau, E., & Mayor, R. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.08.002 · Cited by 186
Transforming Growth Factor-β3 Perturbs the Inter-Sertoli Tight Junction Permeability Barrierin VitroPossibly Mediated via Its Effects on Occludin, Zonula Occludens-1, and Claudin-111
Lui, W., Lee, W. M., & Cheng, C. Y. (2001) · Endocrinology · doi:10.1210/endo.142.5.8116 · Cited by 182
A Differentiation-dependent Splice Variant of Myosin Light Chain Kinase, MLCK1, Regulates Epithelial Tight Junction Permeability
Clayburgh, D. R., Rosen, S., Witkowski, E. D., Wang, F., Blair, S. A., Dudek, S. M., Garcia, J. G. N., Alverdy, J. C., & Turner, J. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408822200 · Cited by 180
Tight Junction, a Platform for Trafficking and Signaling Protein Complexes
Zahraoui, A., Louvard, D., & Galli, T. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.151.5.f31 · Cited by 181
Role of Epithelial Cells in Initiation and Propagation of Intestinal Inflammation. Eliminating the static: tight junction dynamics exposed
Shen, L., & Turner, J. R. (2006) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00439.2005 · Cited by 176
Protein Kinase C Signaling Regulates ZO-1 Translocation and Increased Paracellular Flux of T84 Colonocytes Exposed toClostridium difficile Toxin A
Chen, M. L., Pothoulakis, C., & LaMont, J. T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109254200 · Cited by 172
Occludin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition
Wachtel, M., Frei, K., Ehler, E., Fontana, A., Winterhalter, K. H., & Gloor, S. M. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.23.4347 · Cited by 172
Relationship between Na+,K+-ATPase and cell attachment
Contreras, R. G., Shoshani, L., Flores-Maldonado, C., Lázaro, A., & Cereijido, M. (1999) · Journal of Cell Science · doi:10.1242/jcs.112.23.4223 · Cited by 168
The diverse roles of Rac signaling in tumorigenesis
Mack, N. A., Whalley, H. J., Castillo‐Lluva, S., & Malliri, A. (2011) · Cell Cycle · doi:10.4161/cc.10.10.15612 · Cited by 175
Rho Signaling and Tight Junction Functions
Terry, S. J., Nie, M., Matter, K., & Balda, M. S. (2010) · Physiology · doi:10.1152/physiol.00034.2009 · Cited by 177
Nonreceptor Tyrosine Kinase c-Yes Interacts with Occludin during Tight Junction Formation in Canine Kidney Epithelial Cells
Chen, Y., Lu, Q., Goodenough, D. A., & Jeansonne, B. G. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.01-08-0423 · Cited by 162
Involvement of ASIP/PAR-3 in the promotion of epithelial tight junction formation
Hirose, T., Izumi, Y., Nagashima, Y., Tamai-Nagai, Y., Kurihara, H., Sakai, T., Suzuki, Y., Yamanaka, T., Suzuki, A., Mizuno, K., et al. (2002) · Journal of Cell Science · doi:10.1242/jcs.115.12.2485 · Cited by 162
Rho GTPases and actomyosin: Partners in regulating epithelial cell-cell junction structure and function
Arnold, T. R., Stephenson, R. E., & Miller, A. L. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.03.053 · Cited by 164
The DOCK180/Elmo Complex Couples ARNO-Mediated Arf6 Activation to the Downstream Activation of Rac1
Santy, L. C., Ravichandran, K. S., & Casanova, J. E. (2005) · Current Biology · doi:10.1016/j.cub.2005.08.052 · Cited by 159
Current strategies used to enhance the paracellular transport of therapeutic polypeptides across the intestinal epithelium
Salamat‐Miller, N., & Johnston, T. P. (2005) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2005.01.022 · Cited by 156
Epidermal growth factor receptor pathway substrate 8 (Eps8) is a novel regulator of cell adhesion and the blood‐testis barrier integrity in the seminiferous epithelium
Lie, P. P. Y., Mruk, D. D., Lee, W. M., & Cheng, C. Y. (2009) · The FASEB Journal · doi:10.1096/fj.06-070573 · Cited by 154
Roles of ZO-1, occludin, and actin in oxidant-induced barrier disruption
Musch, M. W., Walsh-Reitz, M. M., & Chang, E. B. (2005) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00301.2005 · Cited by 152
Arp2/3-independent assembly of actin by Vibrio type III effector VopL
Liverman, A. D. B., Cheng, H., Dinalo, J. E., Leung, D. W., Yarbrough, M. L., Burdette, D. L., Rosen, M. K., & Orth, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703196104 · Cited by 150
The role of cell adhesion molecules in ischemic acute renal failure
Molitoris, B. A., & Marrs, J. A. (1999) · The American Journal of Medicine · doi:10.1016/s0002-9343(99)00061-3 · Cited by 146
Chemokines and chemokine receptors in mucosal homeostasis at the intestinal epithelial barrier in inflammatory bowel disease
Zimmerman, N. P., Vongsa, R. A., Wendt, M. K., & Dwinell, M. B. (2008) · Inflammatory Bowel Diseases · doi:10.1002/ibd.20480 · Cited by 147
Human homologues of the Caenorhabditis elegans cell polarity protein PAR6 as an adaptor that links the small GTPases Rac and Cdc42 to atypical protein kinase C
Noda, Y., Takeya, R., Ohno, S., Naito, S., Ito, T., & Sumimoto, H. (2001) · Genes to Cells · doi:10.1046/j.1365-2443.2001.00404.x · Cited by 154
Adenosine receptor signaling: a key to opening the blood–brain door
Bynoe, M. S., Viret, C., Yan, A., & Kim, D.-G. (2015) · Fluids and Barriers of the CNS · doi:10.1186/s12987-015-0017-7 · Cited by 143
Rho/Rho-associated Kinase-II Signaling Mediates Disassembly of Epithelial Apical Junctions
Samarin, S., Ivanov, A. I., Flatau, G., Parkos, C. A., & Nusrat, A. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-04-0315 · Cited by 138
Podocalyxin activates RhoA and induces actin reorganization through NHERF1 and Ezrin in MDCK cells
Schmieder, S., Nagai, M., Orlando, R. A., Takeda, T., & Farquhar, M. G. (2004) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000135968.49899.e8 · Cited by 137
The mammalian homologue of the Caenorhabditis elegans polarity protein PAR-6 is a binding partner for the Rho GTPases Cdc42 and Rac1
Johansson, A.-S., Driessens, M., & Aspenström, P. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.18.3267 · Cited by 146
Endothelial tight junctions: permeable barriers of the vessel wall
Bazzoni, G. (2005) · Thrombosis and Haemostasis · doi:10.1160/th05-07-0488 · Cited by 132
Caffeine Protects Against Disruptions of the Blood-Brain Barrier in Animal Models of Alzheimer's and Parkinson's Diseases
Chen, X., Ghribi, O., & Geiger, J. D. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1376 · Cited by 137
Cdc42-dependent modulation of tight junctions and membrane protein traffic in polarized Madin-Darby canine kidney cells.
Rojas, R., Ruiz, W., Leung, S., Jou, T., & Apodaca, G. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2257 · Cited by 142
Self-citation
The interdependence of the Rho GTPases and apicobasal cell polarity
Mack, N. A., & Georgiou, M. (2014) · Small GTPases · doi:10.4161/21541248.2014.973768 · Cited by 123
JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function
Monteiro, A. C., Sumagin, R., Rankin, C. R., Leoni, G., Mina, M. J., Reiter, D. M., Stehle, T., Dermody, T. S., Schaefer, S. A., Hall, R. A., et al. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-06-0298 · Cited by 129

Authors: Jou, T.-S., Schneeberger, E. E., & James Nelson, W.
Affiliations: Massachusetts General Hospital (US)
*Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305-5345; ‡Department of Pathology, Massachusetts General Hospital, Boston, MA 02114
ORCID: Jou, Tzuu-Shuh
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 1998-07-13
Volume: 142
Issue: 1
Pages: 101-115
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.142.1.101
PMC: PMC2133025
OpenAlex: W2046587126
Cited by: 354
References: 58
Citations by year: 2026: 1 · 2025: 7 · 2024: 5 · 2023: 2 · 2022: 5 · 2021: 6 · 2020: 3 · 2019: 5 · 2018: 3 · 2017: 5 · 2016: 5 · 2015: 4 · 2014: 16 · 2013: 10 · 2012: 14
FWCI: 16.95
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: cc-by-nc-sa
Locations: The Journal of Cell Biology (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Neurology › Barrier Structure and Function Studies
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Keywords: tight junctions, RhoA, Rac1, small GTPases, paracellular permeability, occludin, ZO-1, MDCK cells, epithelial polarity, transepithelial electrical resistance, membrane protein targeting, membrane lateral organization
MeSH terms: Animals, Cell Line, Cell Membrane, Detergents, Dogs, Epithelial Cells, Membrane Proteins, Phosphoproteins, Solubility, Mutagenesis, Octoxynol, Tight Junctions, GTP-Binding Proteins, GTP Phosphohydrolases, rhoA GTP-Binding Protein, rac GTP-Binding Proteins, Occludin, Zonula Occludens-1 Protein, Zonula Occludens-2 Protein

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

Structural and Functional Regulation of Tight Junctions by RhoA and Rac1 Small GTPases

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks