OptoTAT reveals microtubule acetylation as a rapid trigger for GEF-H1–mediated cell migration
Open accessAbstract
Microtubule acetylation is implicated in regulating cell motility, yet its physiological role in directional migration and the underlying molecular mechanisms have remained unclear. This knowledge gap has persisted primarily due to a lack of tools capable of rapidly manipulating microtubule acetylation in actively migrating cells. To overcome this limitation and elucidate the causal relationship between microtubule acetylation and cell migration, we developed a novel optogenetic actuator, optoTAT, which enables precise induction of microtubule acetylation within minutes in live cells. Implementing optoTAT in migration assays, we observed striking and rapid responses at both molecular and cellular levels. First, microtubule acetylation triggers release of the RhoA activator GEF-H1 from sequestration on microtubules. This release subsequently enhances actomyosin contractility and drives focal adhesion maturation. These subcellular processes collectively promote sustained directional migration. Our findings position GEF-H1 as a critical molecular responder to microtubule acetylation, enabling a dynamic crosstalk between the actin and microtubule cytoskeletal networks in the coordination of cellular motility.
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
Cites
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?
GFP-GEF-H1 bound along most microtubules in U2OS cells.
“GFP-GEF-H1 bound along most microtubules in U2OS cells”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [33]
The Results section (‘Microtubule acetylation releases GEF-H1 from sequestration’; page unavailable) reports GEF-H1 associated with microtubules in MEFs and HeLa cells. It does not establish that GFP-GEF-H1 bound along most microtubules in U2OS cells. (LLM, conf=0.85)
Experimental — accuracy not yet measuredGFP-GEF-H1 was barely detected on acetylated microtubules in U2OS cells.
“but was barely detected on acetylated microtubules (Fig. 3a, yellow dashed line, and Fig. 3c)”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [33]
The Results section, under “Microtubule acetylation releases GEF-H1 from sequestration” (page unavailable), reports a negative spatial correlation between microtubule-bound GEF-H1 and acetylated microtubules. That observation was made by immunostaining WT mouse embryonic fibroblasts, not by detecting GFP-GEF-H1 in U2OS cells; the cited paper therefore supports the general localization pattern but not the specified cell type or fluorescent construct. (LLM, conf=0.86)
Experimental — accuracy not yet measuredGEF-H1 avoids acetylated microtubules.
“Previous studies have suggested that GEF-H1 avoids acetylated microtubules 32,33 .”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [33]
In cells, GEF-H1 avoids acetylated, stable microtubules.
“In cells, GEF-H1 avoids acetylated, stable microtubules 32,33 , probably because their lattices are expanded 39,53 and are thus more similar in conformation to paclitaxel- and GMPCPP-stabilized microtubules.”
From Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling (2026) · cites this paper as [33]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Cell Migration: Integrating Signals from Front to Back
Ridley, A. J., Schwartz, M. A., Burridge, K., Firtel, R., Ginsberg, M. H., Borisy, G. G., Parsons, J. T., & Horwitz, A. R. (2003) · Science · doi:10.1126/science.1092053 · Cited by 4,929 · see citing works
HDAC6 is a microtubule-associated deacetylase
Hubbert, C., Guardiola, A., Shao, R., Kawaguchi, Y., Ito, A., Nixon, A., Yoshida, M., Wang, X.-F., & Yao, T.-P. (2002) · Nature · doi:10.1038/417455a · Cited by 2,403 · see citing works
Balaban, N. Q., Schwarz, U. S., Riveline, D., Goichberg, P., Tzur, G., Sabanay, I., Mahalu, D., Safran, S. A., Bershadsky, A. D., Addadi, L., et al. (2001) · Nature Cell Biology · doi:10.1038/35074532 · Cited by 2,137 · see citing works
Non-muscle myosin II takes centre stage in cell adhesion and migration
Vicente‐Manzanares, M., Ma, X., Adelstein, R. S., & Horwitz, A. R. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2786 · Cited by 2,041 · see citing works
Taxol stabilizes microtubules in mouse fibroblast cells.
Schiff, P. B., & Horwitz, S. B. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.3.1561 · Cited by 1,971 · see citing works
Measuring mechanical tension across vinculin reveals regulation of focal adhesion dynamics
Grashoff, C., Hoffman, B. D., Brenner, M. D., Zhou, R., Parsons, M., Yang, M. T., McLean, M. A., Sligar, S. G., Chen, C. S., Ha, T., et al. (2010) · Nature · doi:10.1038/nature09198 · Cited by 1,549 · see citing works
The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase
North, B. J., Marshall, B. L., Borra, M. T., Denu, J. M., & Verdin, E. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00038-8 · Cited by 1,542 · see citing works
HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153 · see citing works
Rezakhaniha, R., Agianniotis, A., Schrauwen, J. T. C., Griffa, A., Sage, D., Bouten, C. V. C., van de Vosse, F. N., Unser, M. A., & Stergiopulos, N. (2011) · Biomechanics and Modeling in Mechanobiology · doi:10.1007/s10237-011-0325-z · Cited by 1,104 · see citing works
Haggarty, S. J., Koeller, K. M., Wong, J. C., Grozinger, C. M., & Schreiber, S. L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0430973100 · Cited by 1,066 · see citing works
Coordination of Rho GTPase activities during cell protrusion
Machacek, M., Hodgson, L., Welch, C. M., Elliott, H. L., Pertz, O. C., Nalbant, P., Abell, A. N., Johnson, G. L., Hahn, K. M., & Danuser, G. M. (2009) · Nature · doi:10.1038/nature08242 · Cited by 1,001 · see citing works
Mechanical Integration of Actin and Adhesion Dynamics in Cell Migration
Gardel, M. L., Schneider, I. C., Aratyn-Schaus, Y., & Waterman, C. M. (2010) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.011209.122036 · Cited by 962 · see citing works
Random versus directionally persistent cell migration
Petrie, R. J., Doyle, A. D., & Yamada, K. M. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2729 · Cited by 956 · see citing works
The tubulin code and its role in controlling microtubule properties and functions
Janke, C., & Magiera, M. M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0214-3 · Cited by 956 · see citing works
Microtubule Acetylation Promotes Kinesin-1 Binding and Transport
Reed, N. A., Cai, D., Blasius, T. L., Jih, G. T., Meyhofer, E., Gaertig, J., & Verhey, K. J. (2006) · Current Biology · doi:10.1016/j.cub.2006.09.014 · Cited by 919 · see citing works
Microtubules containing acetylated alpha-tubulin in mammalian cells in culture.
Piperno, G., LeDizet, M., & Chang, X. J. (1987) · The Journal of cell biology · doi:10.1083/jcb.104.2.289 · Cited by 873 · see citing works
Post-translational regulation of the microtubule cytoskeleton: mechanisms and functions
Janke, C., & Bulinski, J. C. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3227 · Cited by 838 · see citing works
Piperno, G., & Fuller, M. T. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.6.2085 · Cited by 758 · see citing works
HDAC6 Modulates Cell Motility by Altering the Acetylation Level of Cortactin
Zhang, X. M., Yuan, Z., Zhang, Y., Yong, S., Salas-Burgos, A., Koomen, J. M., Olashaw, N., Parsons, J. T., Yang, X., Dent, S., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.033 · Cited by 731 · see citing works
Krendel, M., Zenke, F. T., & Bokoch, G. M. (2002) · Nature Cell Biology · doi:10.1038/ncb773 · Cited by 669 · see citing works
Microtubule-induced focal adhesion disassembly is mediated by dynamin and focal adhesion kinase
Ezratty, E. J., Partridge, M. A., & Gundersen, G. G. (2005) · Nature Cell Biology · doi:10.1038/ncb1262 · Cited by 650 · see citing works
Pasapera, A. M., Schneider, I. C., Rericha, E. C., Schlaepfer, D. D., & Waterman, C. M. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200906012 · Cited by 573 · see citing works
Microtubules acquire resistance from mechanical breakage through intralumenal acetylation
Xu, Z., Schaedel, L., Portran, D., Aguilar, A., Gaillard, J., Marinkovich, M. P., Théry, M., & Nachury, M. V. (2017) · Science · doi:10.1126/science.aai8764 · Cited by 513 · see citing works
Myosin IIA regulates cell motility and actomyosin–microtubule crosstalk
Even‐Ram, S., Doyle, A. D., Conti, M. A., Matsumoto, K., Adelstein, R. S., & Yamada, K. M. (2007) · Nature Cell Biology · doi:10.1038/ncb1540 · Cited by 508 · see citing works
L’Hernault, S. W., & Rosenbaum, J. L. (1985) · Biochemistry · doi:10.1021/bi00323a034 · Cited by 497 · 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
Tubulin acetylation protects long-lived microtubules against mechanical ageing
Portran, D., Schaedel, L., Xu, Z., Théry, M., & Nachury, M. V. (2017) · Nature Cell Biology · doi:10.1038/ncb3481 · Cited by 491 · see citing works
MEC-17 is an α-tubulin acetyltransferase
Akella, J. S., Wloga, D., Kim, J., Starostina, N. G., Lyons-Abbott, S., Morrissette, N. S., Dougan, S. T., Kipreos, E. T., & Gaertig, J. (2010) · Nature · doi:10.1038/nature09324 · Cited by 489 · see citing works
Shida, T., Cueva, J. G., Xu, Z., Goodman, M. B., & Nachury, M. V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013728107 · Cited by 474 · see citing works
Focal adhesions, stress fibers and mechanical tension
Burridge, K., & Guilluy, C. (2016) · Experimental Cell Research · doi:10.1016/j.yexcr.2015.10.029 · Cited by 409 · see citing works
Structural basis for vinculin activation at sites of cell adhesion
Bakolitsa, C., Cohen, D. M., Bankston, L. A., Bobkov, A. A., Cadwell, G. W., Jennings, L., Critchley, D. R., Craig, S. W., & Liddington, R. (2004) · Nature · doi:10.1038/nature02610 · Cited by 384 · see citing works
Effects of α-tubulin acetylation on microtubule structure and stability
Eshun-Wilson, L., Zhang, R., Portran, D., Nachury, M. V., Toso, D. B., Löhr, T., Vendruscolo, M., Bonomi, M., Fraser, J. S., & Nogales, E. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1900441116 · Cited by 366 · see citing works
Identification of an acetylation site of Chlamydomonas alpha-tubulin.
Ledizet, M., & Piperno, G. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.16.5720 · Cited by 319 · see citing works
Causes and Consequences of Microtubule Acetylation
Janke, C., & Montagnac, G. (2017) · Current Biology · doi:10.1016/j.cub.2017.10.044 · Cited by 312 · 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
Maruta, H., Greer, K. L., & Rosenbaum, J. L. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.2.571 · Cited by 267 · see citing works
Microtubules are acetylated in domains that turn over slowly
Webster, D. R., & Borisy, G. G. (1989) · Journal of Cell Science · doi:10.1242/jcs.92.1.57 · Cited by 264 · see citing works
Optogenetic control of nuclear protein export
Niopek, D., Wehler, P., Roensch, J., Eils, R., & Ventura, B. D. (2016) · Nature Communications · doi:10.1038/ncomms10624 · Cited by 249 · see citing works
Identification of genes expressed in C. elegans touch receptor neurons
Zhang, Y., Ma, C., Delohery, T. M., Nasipak, B. T., Foat, B. C., Bounoutas, A., Bussemaker, H. J., Kim, S. K., & Chalfie, M. (2002) · Nature · doi:10.1038/nature00891 · Cited by 246 · see citing works
αTAT1 is the major α-tubulin acetyltransferase in mice
Kalebic, N., Sorrentino, S., Perlas, E., Bolasco, G., Martinez, C., & Heppenstall, P. A. (2013) · Nature Communications · doi:10.1038/ncomms2962 · Cited by 241 · see citing works
Molecular Basis for Age-Dependent Microtubule Acetylation by Tubulin Acetyltransferase
Szyk, A., Deaconescu, A. M., Spector, J., Goodman, B., Valenstein, M. L., Ziolkowska, N. E., Kormendi, V., Grigorieff, N., & Roll-Mecak, A. (2014) · Cell · doi:10.1016/j.cell.2014.03.061 · Cited by 218 · 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
Geeraert, C., Ratier, A., Pfisterer, S. G., Perdiz, D., Cantaloube, I., Rouault, A., Pattingre, S., Proikas‐Cezanne, T., Codogno, P., & Poüs, C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.091553 · Cited by 204 · 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
Bouchet, B. P., Gough, R. E., van de Willige, D., Ammon, Y.-C., Post, H., Jacquemet, G., Altelaar, M. A. F., Heck, A. J. R., Goult, B. T., & Akhmanova, A. S. (2016) · eLife · doi:10.7554/elife.18124 · Cited by 196 · see citing works
Cytoskeletal coherence requires myosin-IIA contractility
Cai, Y., Rossier, O., Gauthier, N. C., Biais, N., Fardin, M.-A., Zhang, X., Miller, L. W., Ladoux, B., Cornish, V. W., & Sheetz, M. P. (2010) · Journal of Cell Science · doi:10.1242/jcs.058297 · Cited by 192 · see citing works
Boggs, A. E., Vitolo, M. I., Whipple, R. A., Charpentier, M. S., Goloubeva, O. G., Ioffe, O. B., Tuttle, K. C., Slovic, J., Lu, Y., Mills, G. B., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-3563 · 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
Sudo, H., & Baas, P. W. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0048-10.2010 · Cited by 181 · 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
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
Taxol-induced flexibility of microtubules and its reversal by MAP-2 and Tau.
Dye, R. B., Fink, S. P., & Williams, R. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53113-6 · Cited by 161 · see citing works
Kim, G.-W., Li, L., Gorbani, M., You, L., & Yang, X.-J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.464792 · Cited by 141 · 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
Tubulin hyperacetylation is adaptive in cardiac proteotoxicity by promoting autophagy
McLendon, P. M., Ferguson, B. S., Osińska, H. E., Bhuiyan, M. S., James, J. F., McKinsey, T. A., & Robbins, J. M. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415589111 · Cited by 121 · see citing works
Mitra, A., & Sept, D. (2008) · Biophysical Journal · doi:10.1529/biophysj.108.133884 · Cited by 119 · see citing works
Luminal Localization of α-tubulin K40 Acetylation by Cryo-EM Analysis of Fab-Labeled Microtubules
Soppina, V., Herbstman, J. F., Skiniotis, G., & Verhey, K. J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048204 · Cited by 116 · see citing works
Castro-Castro, A., Janke, C., Montagnac, G., Paul‐Gilloteaux, P., & Chavrier, P. (2012) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2012.07.001 · Cited by 109 · see citing works
Rooney, C., White, G. R. M., Nazgiewicz, A., Woodcock, S. A., Anderson, K. I., Ballestrem, C., & Malliri, A. (2010) · EMBO Reports · doi:10.1038/embor.2010.10 · Cited by 109 · see citing works
Theisen, U., Straube, E., & Straube, A. (2012) · Developmental Cell · doi:10.1016/j.devcel.2012.11.005 · Cited by 105 · see citing works
Acetylated Microtubules Are Preferentially Bundled Leading to Enhanced Kinesin-1 Motility
Balabanian, L., Berger, C. L., & Hendricks, A. G. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.08.009 · Cited by 103 · see citing works
Esteves, A. R., Palma, A. M., Gomes, R., Santos, D., Silva, D. F., & Cardoso, S. M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.11.014 · Cited by 103 · see citing works
Acetylated tubulin is essential for touch sensation in mice
Morley, S. J., Qi, Y., Iovino, L., Andolfi, L., Guo, D., Kalebic, N., Castaldi, L., Tischer, C., Portulano, C., Bolasco, G., et al. (2016) · eLife · doi:10.7554/elife.20813 · Cited by 102 · see citing works
Microtubules regulate GEF-H1 in response to extracellular matrix stiffness
Heck, J. N., Ponik, S. M., Garcia-Mendoza, M. G., Pehlke, C. A., Inman, D. R., Eliceiri, K. W., & Keely, P. J. (2012) · Molecular Biology of the Cell · doi:10.1091/mbc.e11-10-0876 · Cited by 96 · see citing works
Bance, B., Seetharaman, S., Leduc, C., Boëda, B., & Etienne‐Manneville, S. (2019) · Journal of Cell Science · doi:10.1242/jcs.225805 · Cited by 90 · see citing works
Aguilar, A., Becker, L., Tedeschi, T. R., Heller, S., Iomini, C., & Nachury, M. V. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-10-0609 · Cited by 89 · see citing works
ERK1/2 phosphorylate GEF-H1 to enhance its guanine nucleotide exchange activity toward RhoA
Fujishiro, S., Tanimura, S., Mure, S., Kashimoto, Y., Watanabe, K., & Kohno, M. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.066 · Cited by 84 · see citing works
Efficient Front-Rear Coupling in Neutrophil Chemotaxis by Dynamic Myosin II Localization
Tsai, T. Y.-C., Collins, S. R., Chan, C. K., Hadjitheodorou, A., Lam, P., Lou, S. S., Yang, H. W., Jorgensen, J. A., Ellett, F. E., Irimia, D., et al. (2019) · Developmental Cell · doi:10.1016/j.devcel.2019.03.025 · Cited by 81 · see citing works
Joo, E. E., & Yamada, K. M. (2014) · Nature Communications · doi:10.1038/ncomms4510 · Cited by 73 · see citing works
Han, S. J., Azarova, E. V., Whitewood, A. J., Bachir, A. I., Gutierrez, E., Groisman, A., Horwitz, A. R., Goult, B. T., Dean, K. M., & Danuser, G. M. (2021) · eLife · doi:10.7554/elife.66151 · Cited by 73 · see citing works
Microtubule Acetylation Is Required for Mechanosensation in Drosophila
Yan, C. H., Wang, F., Peng, Y. W., Williams, C., Jenkins, B., Wildonger, J., Kim, H., Perr, J., Vaughan, J. C., Kern, M., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.09.075 · Cited by 73 · see citing works
Meiri, D., Marshall, C. B., Mokady, D., LaRose, J., Mullin, M., Gingras, A.-C., Ikura, M., & Rottapel, R. (2014) · Nature Communications · doi:10.1038/ncomms5857 · Cited by 70 · see citing works
Compression-dependent microtubule reinforcement enables cells to navigate confined environments
Ju, R. J., Falconer, A. D., Schmidt, C. J., Martínez, M. A. E., Dean, K. M., Fiolka, R. P., Sester, D. P., Nobis, M., Timpson, P., Lomakin, A. J., et al. (2024) · Nature Cell Biology · doi:10.1038/s41556-024-01476-x · Cited by 62 · see citing works
Spatiotemporal dynamics of GEF-H1 activation controlled by microtubule- and Src-mediated pathways
Azoitei, M. L., Noh, J., Marston, D. J., Roudot, P., Marshall, C. B., Daugird, T. A., Lisanza, S. L., Sandí, M.-J., Ikura, M., Sondek, J., et al. (2019) · Journal of Cell Biology · doi:10.1083/jcb.201812073 · Cited by 61 · see citing works
Lee, C.-C., Cheng, Y.-C., Chang, C.-Y., Lin, C.-M., & Chang, J. (2018) · Scientific Reports · doi:10.1038/s41598-018-35392-6 · Cited by 51 · see citing works
Optogenetic control of cofilin and αTAT in living cells using Z-lock
Stone, O. J., Pankow, N., Liu, B., Sharma, V. P., Eddy, R. J., Wang, H., Putz, A. T., Teets, F. D., Kuhlman, B. A., Condeelis, J. S., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0405-4 · Cited by 49 · see citing works
Bhuwania, R., Castro-Castro, A., & Linder, S. (2014) · European Journal of Cell Biology · doi:10.1016/j.ejcb.2014.07.006 · Cited by 48 · see citing works
Liu, N., Xiong, Y., Li, S., Ren, Y., He, Q., Gao, S., Zhou, J., & Shui, W. (2015) · Scientific Reports · doi:10.1038/srep16869 · Cited by 48 · see citing works
Fourcade, S., Morató, L., Parameswaran, J., Ruíz, M., Ruiz-Cortés, Z. T., Jové, M., Naudí, A., Martínez‐Redondo, P., Dierssen, M., Ferrer, I., et al. (2017) · Aging Cell · doi:10.1111/acel.12682 · Cited by 48 · see citing works
Precise control of microtubule disassembly in living cells
Liu, G. Y., Chen, S., Lee, G., Shaiv, K., Chen, P., Cheng, H., Hong, S., Yang, W., Huang, S., Chang, Y., et al. (2022) · The EMBO Journal · doi:10.15252/embj.2021110472 · Cited by 45 · see citing works
Distribution of acetylated alpha-tubulin in Physarum polycephalum.
Diggins, M., & Dove, W. F. (1987) · The Journal of Cell Biology · doi:10.1083/jcb.104.2.303 · Cited by 45 · see citing works
Optogenetic activation of Plexin-B1 reveals contact repulsion between osteoclasts and osteoblasts
Deb Roy, A., Yin, T., Choudhary, S., Rodionov, V., Pilbeam, C. C., & Wu, Y. I. (2017) · Nature Communications · doi:10.1038/ncomms15831 · Cited by 44 · see citing works
HDAC6 regulates DNA damage response via deacetylating MLH1
Zhang, M., Chen, H., Moses, N., Haakenson, J., Xiang, S., Quan, D. L., Fang, B., Yang, Z., Bai, W., Bepler, G., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006374 · Cited by 42 · see citing works
Oh, S., You, E., Ko, P., Jeong, J., Keum, S., & Rhee, S. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.11.039 · Cited by 41 · see citing works
Dynamic regulation of GEF-H1 localization at microtubules by Par1b/MARK2
Yoshimura, Y., & Miki, H. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.04.032 · Cited by 39 · see citing works
Pan, W., Nagpal, K., Suárez‐Fueyo, A., Ferretti, A. P., Yoshida, N., Tsokos, M., & Tsokos, G. C. (2021) · The Journal of Immunology · doi:10.4049/jimmunol.2001266 · Cited by 38 · see citing works
p27Kip1 Modulates Axonal Transport by Regulating α-Tubulin Acetyltransferase 1 Stability
Morelli, G., Even, A., Gladwyn-Ng, I. E., Bail, R. L., Shilian, M., Godin, J. D., Peyre, E., Hassan, B. A., Besson, A., Rigo, J., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.083 · Cited by 37 · see citing works
Chen, J., Zhang, J., Shaik, N. F., Yi, B., Wei, X., Yang, X., Naik, U. P., Summer, R. S., Yan, G., Xu, X., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011317 · Cited by 36 · see citing works
Microtubule detyrosination drives symmetry breaking to polarize cells for directed cell migration
Lavrsen, K., Rajendraprasad, G., Leda, M., Eibes, S., Vitiello, E., Katopodis, V., Goryachev, A. B., & Barišić, M. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2300322120 · Cited by 28 · see citing works
Gomes, I. D., Ariyaratne, U. V., & Pflum, M. K. H. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00303 · Cited by 20 · see citing works
Non-catalytic allostery in α-TAT1 by a phospho-switch drives dynamic microtubule acetylation
Roy, A. D., Gross, E. G., Pillai, G. S., Seetharaman, S., Etienne‐Manneville, S., & Inoue, T. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202202100 · Cited by 19 · see citing works
Self-citationThe role of the α-tubulin acetyltransferase αTAT1 in the DNA damage response
Ryu, N.-M., & Kim, J. M. (2020) · Journal of Cell Science · doi:10.1242/jcs.246702 · Cited by 16 · see citing works
Mouawad, F., Aoudjit, L., Jiang, R., Szászi, K., & Takano, T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.506816 · Cited by 14 · see citing works
Siow, D. L., & Wattenberg, B. W. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.05.016 · Cited by 14 · see citing works
Effects of αTAT1 and HDAC5 on axonal regeneration in adult neurons
Lin, S., Sterling, N. A., Junker, I. P., Helm, C. T., & Smith, G. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0177496 · Cited by 13 · see citing works
Lfc subcellular localization and activity is controlled by αv-class integrin
Coló, G. P., Seiwert, A., & Haga, R. B. (2023) · Journal of Cell Science · doi:10.1242/jcs.260740 · Cited by 7 · see citing works
Coleman, A. K., Joca, H. C., Shi, G., Lederer, W. J., & Ward, C. W. (2020) · doi:10.1101/2020.06.10.144931 · Cited by 2
Flagged first, then by citations
Cited by
Sorted by citations
Meiring, J. C. M., Mahapatra, V., Liu, R., Gravett, M. S. C., Morren, D., Saunders, H. A. J., Choi, S. R., Pelster José, A., Karhanova, A., Metallidou, I., et al. (2026) · Nature Cell Biology · doi:10.1038/s41556-026-02079-4
- Authors
- Deb Roy, A., Gonzalez, C. S., Stanislauskas, M., Shahid, F., Yadav, E., Rezek, J., & Inoue, T.
- Affiliations
- Johns Hopkins University School of Medicine 1 Department of Cell Biology and Center for Cell Dynamics, , Baltimore, MD,
- Johns Hopkins University (US)
- Center for Cell Analysis and Modeling, University of Connecticut School of Medicine 3 , Farmington, CT,
- Corresponding author
- Inoue, Takanari
- ORCID
- Venue
- Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2026-03-19
- Volume
- 225
- Issue
- 5
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC13004174
- OpenAlex
- W7138849270
- Cited by
- 2
- References
- 98
- Citations by year
- 2026: 2
- FWCI
- 6.70
- Type
- journal article
- Language
- en
- Open access
- green
- pmc.ncbi.nlm.nih.gov
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (publishedVersion)
- Funders
- National Institutes of Health (R35GM149329, T32GM007445, F31GM153141)
- American Heart Association (23POST1057352)
- D.C. Women’s Board Postdoctoral Fellowship
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Keywords
- microtubule acetylation, GEF-H1, cell migration, optogenetic actuators, RhoA activation, actomyosin contractility, focal adhesion maturation, directional migration, cytoskeletal dynamics
- MeSH terms
- Acetylation, Actomyosin, Animals, Cell Movement, Humans, Microtubules, rhoA GTP-Binding Protein, Focal Adhesions, Optogenetics, Rho Guanine Nucleotide Exchange Factors
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
