Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton
Abstract
Regulation of the actin cytoskeleton by microtubules is mediated by the Rho family GTPases. However, the molecular mechanisms that link microtubule dynamics to Rho GTPases have not, as yet, been identified. Here we show that the Rho guanine nucleotide exchange factor (GEF)-H1 is regulated by an interaction with microtubules. GEF-H1 mutants that are deficient in microtubule binding have higher activity levels than microtubule-bound forms. These mutants also induce Rho-dependent changes in cell morphology and actin organization. Furthermore, drug-induced microtubule depolymerization induces changes in cell morphology and gene expression that are similar to the changes induced by the expression of active forms of GEF-H1. Furthermore, these effects are inhibited by dominant-negative versions of GEF-H1. Thus, GEF-H1 links changes in microtubule integrity to Rho-dependent regulation of the actin cytoskeleton.
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GEF-H1 is sequestered on microtubules in an inactive form and becomes active upon release from microtubules.
“This effect depends on the RhoA activator guanine nucleotide exchange factor H1 (GEF-H1), which is sequestered on microtubules in an inactive form, but becomes active upon release from microtubules 18-22 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [18]
RhoA activation by microtubule-destabilizing agents depends on GEF-H1.
“This effect depends on the RhoA activator guanine nucleotide exchange factor H1 (GEF-H1), which is sequestered on microtubules in an inactive form, but becomes active upon release from microtubules 18-22 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [18]
Microtubule-destabilizing agents activate GEF-H1 by inducing its unbinding from microtubules.
“As microtubule-destabilizing agents activate GEF-H1 by inducing its unbinding from microtubules 18-21”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [18]
GEF-H1 catalytic activity is uniquely regulated by its localization to microtubules.
“Of the several classes of GEF, the catalytic activity of GEF-H1 is uniquely regulated by its localization to the microtubules.”
From Expression of Tau Produces Aberrant Plasma Membrane Blebbing in Glial Cells Through RhoA-ROCK-Dependent F-Actin Remodeling (2016) · cites this paper as [43]
Microtubules sequester GEFH1, rendering it inactive, and depolymerization releases GEFH1, activating RhoA.
“Microtubules sequester GEFH1, rendering it inactive, and depolymerization releases GEFH1, activating RhoA.”
From Structural basis of microtubule-mediated signal transduction (2026) · cites this paper as [10]
Wild-type GEFH1 FL co-localized and bundled microtubules, while the FL-C53R mutant and the FL-αβ, FL-α′β′, and FL-ββ′ mutants showed perturbed microtubule co-localization.
“wild-type FL co-localized and bundled microtubules, consistent with its known microtubule-associated protein behavior”
From Structural basis of microtubule-mediated signal transduction (2026) · cites this paper as [10]
GEFH1 is a critical microtubule-regulated activator of Rho signaling pathways.
“GEFH1; also known as Arhgef2 or Lfc), a critical microtubule-regulated activator of Rho signaling pathways.”
From Structural basis of microtubule-mediated signal transduction (2026) · cites this paper as [10]
Microtubule-destabilizing agents trigger Rho signaling through GEFH1 release.
“explaining the mechanism by which microtubule-destabilizing agents trigger Rho signaling through GEFH1 release.10”
From Structural basis of microtubule-mediated signal transduction (2026) · cites this paper as [10]
The inter-protofilament binding mode clarifies how GEFH1 can promote microtubule stability independently of RhoA activation.
“The inter-protofilament binding mode further clarifies how GEFH1 can promote microtubule stability independently of RhoA activation.10”
From Structural basis of microtubule-mediated signal transduction (2026) · cites this paper as [10]
LPA or thrombin signalling through Ga12/13 subunits induces stress fibres in a manner that requires GEF-H1.
“LPA or thrombin signalling through Ga 12/13 subunits induces stress fibres in a manner that requires GEF-H1 (ref.5), yet GEF-H1 does not have an identifiable RGS domain.”
From Mechanistic insight into GPCR-mediated activation of the microtubule-associated RhoA exchange factor GEF-H1 (2014) · cites this paper as [5]
Nocodazole-induced microtubule depolymerization potently activates GEF-H1.
“Nocodozole-induced microtubule depolymerization potently activates GEF-H1 (refs 5-7), thus GEF-H1 activity during mitosis may be a consequence of the change in microtubule dynamics during the reorganization of stable interphase microtubules into the mitotic spindle 36 .”
From Mechanistic insight into GPCR-mediated activation of the microtubule-associated RhoA exchange factor GEF-H1 (2014) · cites this paper as [5]
Cites
Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension
Uehata, M., Ishizaki, T., Satoh, H., Ono, T., Kawahara, T., Morishita, T., Tamakawa, H., Yamagami, K., Inui, J., Maekawa, M., et al. (1997) · Nature · doi:10.1038/40187 · Cited by 2,862 · see citing works
Regulation of the small GTP‐binding protein Rho by cell adhesion and the cytoskeleton
Ren, X. D., Kiosses, W. B., & Schwartz, M. A. (1999) · The EMBO Journal · doi:10.1093/emboj/18.3.578 · Cited by 1,573 · see citing works
The Rho family GTPases RhoA, Racl , and CDC42Hsregulate transcriptional activation by SRF
Hill, C. S., Wynne, J., & Treisman, R. (1995) · Cell · doi:10.1016/s0092-8674(05)80020-0 · Cited by 1,269 · see citing works
Nagase, T. (1998) · DNA Research · doi:10.1093/dnares/5.1.31 · Cited by 845 · see citing works
Direct Stimulation of the Guanine Nucleotide Exchange Activity of p115 RhoGEF by Gα 13
Hart, M. J., Jiang, X., Kozasa, T., Roscoe, W., Singer, W. D., Gilman, A. G., Sternweis, P. C., & Bollag, G. E. (1998) · Science · doi:10.1126/science.280.5372.2112 · Cited by 780 · see citing works
Planat‐Benard, V., Bohl, B. P., & Bokoch, G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.19.13198 · Cited by 757 · see citing works
Self-citationSchultz, D., Friedman, J. R., & Rauscher, F. J. (2001) · Genes & Development · doi:10.1101/gad.869501 · Cited by 530 · see citing works
Microtubule growth activates Rac1 to promote lamellipodial protrusion in fibroblasts
Waterman-Storer, C. M., Worthylake, R. A., Liu, B. P., Burridge, K., & Salmon, E. D. (1999) · Nature Cell Biology · doi:10.1038/9018 · Cited by 491 · see citing works
Cell motility: can Rho GTPases and microtubules point the way?
Wittmann, T., & Waterman, C. M. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.21.3795 · Cited by 449 · see citing works
Fukuhara, S., Murga, C., Zohar, M., Igishi, T., & Gutkind, J. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.9.5868 · Cited by 391 · see citing works
Effect of colcemid on the locomotory behaviour of fibroblasts
Vasiliev, J. M., Gelfand, I. M., Domnina, L. V., Ivanova, O. Y., Sg, K., & Olshevskaja, L. V. (1970) · Development · doi:10.1242/dev.24.3.625 · Cited by 341 · see citing works
Timing of cyclin D1 expression within G1 phase is controlled by Rho
Welsh, C. F., Roovers, K., Villanueva, J., Liu, Y., Schwartz, M. A., & Assoian, R. K. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-950 · Cited by 323 · see citing works
Fibroblast contractility and actin organization are stimulated by microtubule inhibitors
Danowski, B. A. (1989) · Journal of Cell Science · doi:10.1242/jcs.93.2.255 · Cited by 308 · see citing works
Ren, Y., Li, R., Zheng, Y., & Busch, H. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.52.34954 · Cited by 295 · see citing works
A requirement for Rho and Cdc42 during cytokinesis in Xenopus embryos
Drechsel, D. N., Hyman, A. A., Hall, A., & Glotzer, M. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00023-6 · Cited by 258 · see citing works
Cook, T. A., Nagasaki, T., & Gundersen, G. G. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.141.1.175 · Cited by 256 · see citing works
Mira, J., Planat‐Benard, V., Groffen, J., Sanders, L. C., & Knaus, U. G. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.1.185 · Cited by 240 · see citing works
King, C. C., Gardiner, E. M. M., Zenke, F. T., Bohl, B. P., Newton, A. C., Hemmings, B. A., & Bokoch, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006553200 · Cited by 235 · see citing works
Self-citationLiao, G., Nagasaki, T., & Gundersen, G. G. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.11.3473 · Cited by 222 · see citing works
Enomoto, T. (1996) · Cell Structure and Function · doi:10.1247/csf.21.317 · Cited by 218 · see citing works
Liu, B. P., Chrzanowska‐Wodnicka, M., & Burridge, K. (1998) · Cell Communication & Adhesion · doi:10.3109/15419069809040295 · Cited by 201 · see citing works
Analysis of MAP 4 function in living cells using green fluorescent protein (GFP) chimeras.
Olson, K. R., McIntosh, J. R., & Olmsted, J. B. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.130.3.639 · Cited by 197 · see citing works
Bulinski, J. C., Richards, J. E., & Piperno, G. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.106.4.1213 · Cited by 174 · see citing works
van Horck, F. P. G., Ahmadian, M. R., Haeusler, L. C., Moolenaar, W. H., & Kranenburg, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m003839200 · Cited by 174 · see citing works
Ishikawa, K.-I. (1998) · DNA Research · doi:10.1093/dnares/5.3.169 · Cited by 163 · see citing works
Glaven, J. A., Whitehead, I., Bagrodia, S., Kay, R., & Cerione, R. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.4.2279 · Cited by 156 · see citing works
Glaven, J. A., Whitehead, I. P., Nomanbhoy, T. K., Kay, R. J., & Cerione, R. A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.44.27374 · Cited by 129 · see citing works
The Small GTP-binding Protein Rho Regulates Cortical Activities in Cultured Cells during Division
O’Connell, C. B., Wheatley, S. P., Ahmed, S., & Wang, Y. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.144.2.305 · Cited by 126 · see citing works
Bershadsky, A. D., Vaisberg, E. A., & Vasiliev, J. M. (1991) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970190303 · Cited by 105 · see citing works
Sterpetti, P., Hack, A. A., Bashar, M. P., Park, B., Cheng, S., Knoll, J. H. M., Urano, T., Feig, L. A., & Toksoz, D. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.2.1334 · Cited by 76 · see citing works
Microtubule-actomyosin interactions in cortical flow and cytokinesis
Mandato, C. A., Benink, H. A., & Bement, W. M. (2000) · Cell Motility and the Cytoskeleton · doi:10.1002/(sici)1097-0169(200002)45:2 · Cited by 69 · see citing works
[11] Measurement of nucleotide exchange and hydrolysis activities in immunoprecipitates
Downward, J. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(95)55013-5 · Cited by 20 · see citing works
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Somlyo, A. P., & Somlyo, A. V. (2003) · Physiological Reviews · doi:10.1152/physrev.00023.2003 · Cited by 1,980 · see citing works
Signaling Mechanisms Regulating Endothelial Permeability
Mehta, D., & Malik, A. B. (2005) · Physiological Reviews · doi:10.1152/physrev.00012.2005 · Cited by 1,711 · see citing works
Cellular mechanotransduction: putting all the pieces together again
Ingber, D. E. (2006) · The FASEB Journal · doi:10.1096/fj.05-5424rev · Cited by 1,627 · see citing works
GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors
Rossman, K. L., Der, C. J., & Sondek, J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1587 · Cited by 1,697 · see citing works
Tight junctions: from simple barriers to multifunctional molecular gates
Zihni, C., Mills, C., Matter, K., & Balda, M. S. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.80 · Cited by 1,484 · see citing works
Biology of the p21-Activated Kinases
Bokoch, G. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161742 · Cited by 1,080 · see citing works
Self-citationCellular Mechanotransduction: From Tension to Function
Martino, F. D., Perestrelo, A. R., Vinarský, V., Pagliari, S., & Forte, G. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00824 · Cited by 958 · see citing works
Adhesion-Dependent Cell Mechanosensitivity
Bershadsky, A. D., Balaban, N. Q., & Geiger, B. (2003) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.19.111301.153011 · Cited by 858 · see citing works
Conserved microtubule–actin interactions in cell movement and morphogenesis
Rodriguez, O. C., Schaefer, A. W., Mandato, C. A., Forscher, P., Bement, W. M., & Waterman-Storer, C. M. (2003) · Nature Cell Biology · doi:10.1038/ncb0703-599 · Cited by 844 · see citing works
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 · see citing works
Hydrostatic pressure and the actomyosin cortex drive mitotic cell rounding
Stewart, M. P., Helenius, J. H., Toyoda, Y., Ramanathan, S. P., Müller, D. J., & Hyman, A. A. (2010) · Nature · doi:10.1038/nature09642 · Cited by 679 · see citing works
Brown, M. C., & Turner, C. E. (2004) · Physiological Reviews · doi:10.1152/physrev.00002.2004 · Cited by 601 · 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 GTPase signaling complexes in cell migration and invasion
Lawson, C. D., & Ridley, A. J. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201612069 · Cited by 539 · see citing works
Microtubules in Cell Migration
Etienne‐Manneville, S. (2013) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-101011-155711 · Cited by 507 · see citing works
The Cytoskeleton—A Complex Interacting Meshwork
Hohmann, T., & Dehghani, F. (2019) · Cells · doi:10.3390/cells8040362 · Cited by 463 · see citing works
Animal Cytokinesis: From Parts List to Mechanisms
Eggert, U., Mitchison, T. J., & Field, C. M. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.74.082803.133425 · Cited by 439 · see citing works
Systemic administration of epothilone B promotes axon regeneration after spinal cord injury
Ruschel, J., Hellal, F., Flynn, K. C., Dupraz, S., Elliott, D. A., Tedeschi, A., Bates, M., Sliwinski, C., Brook, G. A., Dobrindt, K., et al. (2015) · Science · doi:10.1126/science.aaa2958 · Cited by 433 · see citing works
Beyond polymer polarity: how the cytoskeleton builds a polarized cell
Li, R., & Gundersen, G. G. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2522 · Cited by 372 · see citing works
The Rho GEFs LARG and GEF-H1 regulate the mechanical response to force on integrins
Guilluy, C., Swaminathan, V., García‐Mata, R., O’Brien, E. T., Superfine, R., & Burridge, K. (2011) · Nature Cell Biology · doi:10.1038/ncb2254 · Cited by 369 · see citing works
The Pyrin Inflammasome in Health and Disease
Schnappauf, O., Chae, J. J., Kastner, D. L., & Aksentijevich, I. A. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01745 · Cited by 365 · see citing works
Role of GTPases in control of microvascular permeability
Spindler, V., Schlegel, N., & Waschke, J. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq086 · Cited by 362 · see citing works
GEF-H1 Couples Nocodazole-induced Microtubule Disassembly to Cell Contractility via RhoA
Chang, Y.-C., Nalbant, P., Birkenfeld, J., Chang, Z.-F., & Bokoch, G. (2008) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-12-1269 · Cited by 357 · see citing works
Self-citationEsnault, C., Stewart, A., Gualdrini, F., East, P., Horswell, S. D., Matthews, N., & Treisman, R. (2014) · Genes & Development · doi:10.1101/gad.239327.114 · Cited by 355 · see citing works
Concentric zones of active RhoA and Cdc42 around single cell wounds
Benink, H. A., & Bement, W. M. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200411109 · Cited by 336 · see citing works
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 · see citing works
Curvotaxis directs cell migration through cell-scale curvature landscapes
Pieuchot, L., Marteau, J., Guignandon, A., Santos, T. D., Brigaud, I., Chauvy, P.-F., Cloâtre, T., Ponche, A., Petithory, T., Rougerie, P., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06494-6 · Cited by 299 · see citing works
RhoA is required for cortical retraction and rigidity during mitotic cell rounding
Maddox, A. S., & Burridge, K. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200207130 · Cited by 297 · see citing works
The actin cytoskeleton in endothelial cell phenotypes
Prasain, N., & Stevens, T. (2008) · Microvascular Research · doi:10.1016/j.mvr.2008.09.012 · Cited by 287 · see citing works
Remodeling the Cytoskeleton for Growth and Form: An Overview with Some New Views
Wasteneys, G. O., & Galway, M. E. (2003) · Annual Review of Plant Biology · doi:10.1146/annurev.arplant.54.031902.134818 · Cited by 285 · see citing works
Growth Cone Turning Induced by Direct Local Modification of Microtubule Dynamics
Buck, K. B., & Zheng, J. Q. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-21-09358.2002 · Cited by 283 · see citing works
Regulation of cell migration by dynamic microtubules
Kaverina, I., & Straube, A. (2011) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2011.09.017 · Cited by 273 · see citing works
The cytoskeleton in phagocytosis and macropinocytosis
Mylvaganam, S., Freeman, S. A., & Grinstein, S. (2021) · Current Biology · doi:10.1016/j.cub.2021.01.036 · Cited by 263 · see citing works
Molli, P. R., Li, D. Q., Murray, B. W., Rayala, S. K., & Kumar, R. (2009) · Oncogene · doi:10.1038/onc.2009.119 · Cited by 257 · see citing works
Asymmetric focal adhesion disassembly in motile cells
Broussard, J. A., Webb, D. J., & Kaverina, I. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2007.10.009 · Cited by 252 · see citing works
Lippert, J. W. I. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2006.10.020 · Cited by 246 · see citing works
Targeting and transport: How microtubules control focal adhesion dynamics
Stehbens, S., & Wittmann, T. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201206050 · Cited by 244 · see citing works
Microtubule-induced cortical cell polarityPreprint
Siegrist, S. E., & Doe, C. Q. (2007) · Genes & Development · doi:10.1101/gad.1511207 · Cited by 239 · see citing works
Terry, S. J., Zihni, C., Elbediwy, A., Vitiello, E., San, I. V. L. C., Balda, M. S., & Matter, K. (2011) · Nature Cell Biology · doi:10.1038/ncb2156 · Cited by 238 · see citing works
Actin and microtubules in neurite initiation: Are MAPs the missing link?
Dehmelt, L., & Halpain, S. (2003) · Journal of Neurobiology · doi:10.1002/neu.10284 · Cited by 236 · see citing works
GEF-H1 Modulates Localized RhoA Activation during Cytokinesis under the Control of Mitotic Kinases
Birkenfeld, J., Nalbant, P., Bohl, B. P., Pertz, O. C., Hahn, K. M., & Bokoch, G. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.03.014 · Cited by 235 · see citing works
Self-citationCortical Actomyosin Breakage Triggers Shape Oscillations in Cells and Cell Fragments
Paluch, E. K., Piel, M., Prost, J., Bornens, M., & Sykes, C. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.060590 · Cited by 231 · see citing works
Assembly and mechanosensory function of focal adhesions: experiments and models
Bershadsky, A. D., Ballestrem, C., Carramusa, L., Zilberman, Y., Gilquin, B., Khochbin, S., Alexandrova, A. Y., Verkhovsky, A. B., Shemesh, T., & Kozlov, M. M. (2005) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2005.11.001 · Cited by 229 · see citing works
14-3-3 Regulates Actin Dynamics by Stabilizing Phosphorylated Cofilin
Gohla, A., & Bokoch, G. (2002) · Current Biology · doi:10.1016/s0960-9822(02)01184-3 · Cited by 227 · see citing works
Self-citationLim, Y., Lim, S., Tomar, A., Gardel, M. L., Bernard‐Trifilo, J. A., Chen, X. L., Uryu, S. A., Cañete-Soler, R., Zhai, J., Lin, H., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200708194 · Cited by 215 · see citing works
Self-citationMicrotubules and growth cone function
Gordon‐Weeks, P. R. (2003) · Journal of Neurobiology · doi:10.1002/neu.10266 · Cited by 213 · see citing works
Özen, S., Batu, E. D., & Demir, S. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00253 · Cited by 213 · see citing works
Microtubules meet substrate adhesions to arrange cell polarity
Small, J. V., & Kaverina, I. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(02)00008-x · Cited by 211 · see citing works
Microtubules tune mechanosensitive cell responses
Seetharaman, S., Vianay, B., Roca, V., Farrugia, A. J., De Pascalis, C., Boëda, B., Dingli, F., Loew, D., Vassilopoulos, S., Bershadsky, A., et al. (2022) · Nature Materials · doi:10.1038/s41563-021-01108-x · Cited by 210 · see citing works
Arf6 and microtubules in adhesion-dependent trafficking of lipid rafts
Balasubramanian, N., Scott, D. W., Castle, J. D., Casanova, J. E., & Schwartz, M. A. (2007) · Nature Cell Biology · doi:10.1038/ncb1657 · Cited by 209 · see citing works
Mechanosensation through integrins: Cells act locally but think globally
Ingber, D. E. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0530201100 · Cited by 209 · 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
How do microtubules guide migrating cells?
Small, J. V., Geiger, B., Kaverina, I., & Bershadsky, A. D. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm971 · Cited by 205 · see citing works
Aijaz, S., D’Atri, F., Citi, S., Balda, M. S., & Matter, K. (2005) · Developmental Cell · doi:10.1016/j.devcel.2005.03.003 · Cited by 226 · see citing works
Driving Rho GTPase activity in endothelial cells regulates barrier integrity
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Akhmanova, A. S., & Hoogenraad, C. C. (2015) · Current Biology · doi:10.1016/j.cub.2014.12.027 · Cited by 202 · see citing works
Novel role of microtubules in thrombin‐induced endothelial barrier dysfunction
Birukova, A. A., Birukov, K. G., Smurova, K. M., Adyshev, D. M., Kaibuchi, K., Alieva, I. B., Garcia, J. G. N., & Verin, A. D. (2004) · The FASEB Journal · doi:10.1096/fj.04-2328com · Cited by 202 · see citing works
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 · see citing works
Kourtidis, A., Ngok, S. P., & Anastasiadis, P. Z. (2013) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-394311-8.00018-2 · Cited by 201 · see citing works
Microtubules in cell migration
Garcin, C. L., & Straube, A. (2019) · Essays in Biochemistry · doi:10.1042/ebc20190016 · Cited by 200 · see citing works
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 199 · see citing works
Vimentin intermediate filaments control actin stress fiber assembly through GEF-H1 and RhoA
Jiu, Y., Peränen, J., Schaible, N., Cheng, F., Eriksson, J., Krishnan, R., & Lappalainen, P. (2017) · Journal of Cell Science · doi:10.1242/jcs.196881 · Cited by 198 · see citing works
Birukova, A. A., Smurova, K. M., Birukov, K. G., Usatyuk, P. V., Liu, F., Kaibuchi, K., Ricks‐Cord, A., Natarajan, V., Alieva, I. B., Garcia, J. G. N., et al. (2004) · Journal of Cellular Physiology · doi:10.1002/jcp.20055 · Cited by 191 · see citing works
Birkenfeld, J., Nalbant, P., Yoon, S.-H., & Bokoch, G. M. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.02.006 · Cited by 190 · see citing works
Self-citationDechant, R. C., & Glotzer, M. (2003) · Developmental Cell · doi:10.1016/s1534-5807(03)00057-1 · Cited by 189 · see citing works
Burckhardt, C. J., Suomalainen, M., Schoenenberger, P., Boucke, K., Hemmi, S., & Greber, U. F. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.07.006 · Cited by 181 · see citing works
Zenke, F. T., Krendel, M., DerMardirossian, C. M., King, C. C., Bohl, B. P., & Bokoch, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m400084200 · Cited by 181 · see citing works
Self-citationByrne, K. M., Monsefi, N., Dawson, J. C., Degasperi, A., Wills, J. C., Volinsky, N., Dobrzyński, M., Birtwistle, M. R., Tsyganov, M. A., Kiyatkin, A. B., et al. (2016) · Cell Systems · doi:10.1016/j.cels.2016.01.003 · Cited by 174 · see citing works
Orientation and function of the nuclear–centrosomal axis during cell migration
Luxton, G. W. G., & Gundersen, G. G. (2011) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2011.08.001 · Cited by 169 · see citing works
A mechano-signalling network linking microtubules, myosin IIA filaments and integrin-based adhesions
Rafiq, N. M., Nishimura, Y., Plotnikov, S. V., Thiagarajan, V., Zhang, Z., Shi, S., Natarajan, M., Viasnoff, V., Kanchanawong, P., Jones, G. E., et al. (2019) · Nature Materials · doi:10.1038/s41563-019-0371-y · Cited by 167 · see citing works
Nanometer targeting of microtubules to focal adhesions
Krylyshkina, O., Anderson, K. I., Kaverina, I., Upmann, I., Manstein, D. J., Small, J. V., & Toomre, D. K. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200301102 · Cited by 167 · see citing works
P115 RhoGEF and microtubules decide the direction apoptotic cells extrude from an epithelium
Slattum, G. M., McGee, K., & Rosenblatt, J. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200903079 · Cited by 165 · see citing works
Microtubules Regulate Migratory Polarity through Rho/ROCK Signaling in T Cells
Takesono, A., Heasman, S. J., Wojciak-Stothard, B., Garg, R., & Ridley, A. J. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008774 · Cited by 170 · see citing works
Serum response factor controls neuronal circuit assembly in the hippocampus
Knöll, B., Kretz, O., Fiedler, C., Alberti, S., Schütz, G., Frotscher, M., & Nordheim, A. (2006) · Nature Neuroscience · doi:10.1038/nn1627 · Cited by 162 · see citing works
GEF-H1 is involved in agonist-induced human pulmonary endothelial barrier dysfunction
Birukova, A. A., Adyshev, D., Gorshkov, B., Bokoch, G. M., Birukov, K. G., & Verin, A. D. (2006) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00259.2005 · Cited by 173 · see citing works
Self-citationMicrotubules and actin crosstalk in cell migration and division
Akhshi, T. K., Wernike, D., & Piekny, A. J. (2013) · Cytoskeleton · doi:10.1002/cm.21150 · Cited by 157 · see citing works
LIM Kinase 1 Coordinates Microtubule Stability and Actin Polymerization in Human Endothelial Cells
Gorovoy, M. S., Niu, J., Bernard, O., Profirovic, J., Minshall, R. D., Neamu, R. F., & Voyno-Yasenetskaya, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502921200 · Cited by 156 · see citing works
PAK4 mediates morphological changes through the regulation of GEF-H1
Callow, M. G., Zozulya, S., Gishizky, M. L., Jallal, B., & Smeal, T. (2005) · Journal of Cell Science · doi:10.1242/jcs.02313 · Cited by 169 · see citing works
Patterning of the cell cortex by Rho GTPases
Bement, W. M., Goryachev, A. B., Miller, A. L., & von Dassow, G. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00682-z · Cited by 152 · see citing works
Functional versatility of transcription factors in the nervous system: the SRF paradigm
Knöll, B., & Nordheim, A. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2009.05.004 · Cited by 150 · see citing works
Nalbant, P., Chang, Y.-C., Birkenfeld, J., Chang, Z.-F., & Bokoch, G. M. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e09-01-0041 · Cited by 148 · see citing works
Self-citationMemo mediates ErbB2-driven cell motility
Marone, R., Heß, D., Dankort, D. L., Muller, W. J., Hynes, N. E., & Badache, A. (2004) · Nature Cell Biology · doi:10.1038/ncb1134 · Cited by 146 · see citing works
Enteropathogenic Escherichia coli activates the RhoA signaling pathway via the stimulation of GEF‐H1
Matsuzawa, T., Kuwae, A., Yoshida, S., Sasakawa, C., & Abe, A. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600359 · Cited by 145 · see citing works
Oxidative Stress Contributes to Lung Injury and Barrier Dysfunction via Microtubule Destabilization
Kratzer, E., Tian, Y., Sarich, N. A., Wu, T., Meliton, A. Y., Leff, A. R., & Birukova, A. A. (2012) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2012-0161oc · Cited by 142 · see citing works
Tabdanov, E. D., Rodríguez-Merced, N. J., Cartagena‐Rivera, A. X., Puram, V. V., Callaway, M. K., Ensminger, E. A., Pomeroy, E. J., Yamamoto, K., Lahr, W. S., Webber, B. R., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22985-5 · Cited by 142 · see citing works
Dynamic modes of the cortical actomyosin gel during cell locomotion and division
Paluch, E. K., Sykes, C., Prost, J., & Bornens, M. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.11.003 · Cited by 142 · see citing works
The challenges of abundance: epithelial junctions and small GTPase signalling
Braga, V. M. M., & Yap, A. S. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.08.012 · Cited by 139 · see citing works
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 · see citing works
The emerging importance of group II PAKs
Wells, C. M., & Jones, G. E. (2010) · Biochemical Journal · doi:10.1042/bj20091173 · Cited by 137 · see citing works
Epac: effectors and biological functions
Roscioni, S. S., Elzinga, C. R. S., & Schmidt, M. (2008) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-007-0246-7 · Cited by 137 · see citing works
Ryan, X. P., Alldritt, J., Svenningsson, P., Allen, P. B., Wu, G.-Y., Nairn, A. C., & Greengard, P. (2005) · Neuron · doi:10.1016/j.neuron.2005.05.013 · Cited by 142 · see citing works
How actin filaments and microtubules steer growth cones to their targets
Zhou, F., & Cohan, C. S. (2003) · Journal of Neurobiology · doi:10.1002/neu.10278 · Cited by 129 · see citing works
Subversion of actin dynamics by EPEC and EHEC
Caron, E., Crepin, V. F., Simpson, N., Knutton, S., Garmendia, J., & Frankel, G. M. (2006) · Current Opinion in Microbiology · doi:10.1016/j.mib.2005.12.008 · Cited by 128 · see citing works
Wolfenson, H., Henis, Y. I., Geiger, B., & Bershadsky, A. D. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20410 · Cited by 127 · see citing works
Microtubules control cellular shape and coherence in amoeboid migrating cells
Kopf, A., Renkawitz, J., Hauschild, R., Girkontaite, I., Tedford, K., Merrin, J., Thorn-Seshold, O., Trauner, D., Häcker, H., Fischer, K.-D., et al. (2020) · Journal of Cell Biology · doi:10.1083/jcb.201907154 · Cited by 125 · see citing works
Generation and regulation of microtubule network asymmetry to drive cell polarity
Meiring, J. C. M., Shneyer, B. I., & Akhmanova, A. S. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2019.10.004 · Cited by 124 · see citing works
A novel GRK2/HDAC6 interaction modulates cell spreading and motility
Lafarga, V., Aymerich, I., Tapia, O., Mayor, F., & Penela, P. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.466 · Cited by 123 · see citing works
Neutrophil microtubules suppress polarity and enhance directional migration
Xu, J., Wang, F., Keymeulen, A. V., Rentel, M., & Bourne, H. R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0502106102 · Cited by 122 · see citing works
Microtubule motors control membrane dynamics of Salmonella-containing vacuoles
Guignot, J., Caron, E., Beuzón, C. R., Bucci, C., Kagan, J. C., Roy, C. R., & Holden, D. W. (2004) · Journal of Cell Science · doi:10.1242/jcs.00949 · Cited by 121 · see citing works
Kása, A., Csoŕtos, C., & Verin, A. D. (2014) · Tissue Barriers · doi:10.4161/21688370.2014.974448 · Cited by 119 · see citing works
- Authors
- Krendel, M., Zenke, F. T., & Bokoch, G. M.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- Bokoch, Gary M.
- Venue
- Nature Cell Biology
- Published
- 2002-03-25
- Volume
- 4
- Issue
- 4
- Pages
- 294-301
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2055236272
- Cited by
- 669
- References
- 32
- Citations by year
- 2026: 21 · 2025: 29 · 2024: 32 · 2023: 32 · 2022: 22 · 2021: 31 · 2020: 28 · 2019: 36 · 2018: 20 · 2017: 39 · 2016: 29 · 2015: 21 · 2014: 25 · 2013: 37 · 2012: 34
- FWCI
- 11.40
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Cancer Research Institute
- Arthritis Foundation
- Thailand Science Research and Innovation
- U.S. Army
- U.S. Public Health Service
- National Institute of General Medical Sciences (GM34934)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- GEF-H1, RhoGEF, microtubules, actin cytoskeleton, Rho GTPases, microtubule binding, microtubule depolymerization, cell morphology, actin organization
- MeSH terms
- Actins, Animals, Dose-Response Relationship, Drug, Gene Expression Regulation, Guanine Nucleotides, HeLa Cells, Humans, Microscopy, Fluorescence, Microtubule-Associated Proteins, Microtubules, Models, Genetic, Plasmids, Precipitin Tests, Time Factors, Transfection, Protein Structure, Tertiary, Genes, Reporter, DNA, Complementary, COS Cells, Guanine Nucleotide Exchange Factors, ras Guanine Nucleotide Exchange Factors, ras GTPase-Activating Proteins, rhoA GTP-Binding Protein, cdc42 GTP-Binding Protein, rac1 GTP-Binding Protein, Rho Guanine Nucleotide Exchange Factors
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