{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T08:41:20Z","timestamp":1790671280264,"version":"4.1.0"},"reference-count":41,"publisher":"Springer Science and Business Media LLC","issue":"8","license":[{"start":{"date-parts":[[2021,5,3]],"date-time":"2021-05-03T00:00:00Z","timestamp":1620000000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"},{"start":{"date-parts":[[2021,5,3]],"date-time":"2021-05-03T00:00:00Z","timestamp":1620000000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/www.springernature.com\/gp\/researchers\/text-and-data-mining"}],"funder":[{"DOI":"10.13039\/100000057","name":"U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01GM123130"],"award-info":[{"award-number":["R01GM123130"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000057","name":"U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences","doi-asserted-by":"publisher","award":["R01GM136858"],"award-info":[{"award-number":["R01GM136858"]}],"id":[{"id":"10.13039\/100000057","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Nat Chem Biol"],"published-print":{"date-parts":[[2021,8]]},"DOI":"10.1038\/s41589-021-00791-w","type":"journal-article","created":{"date-parts":[[2021,5,3]],"date-time":"2021-05-03T16:03:40Z","timestamp":1620057820000},"page":"888-895","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["A molecular trap inside microtubules probes luminal access by soluble proteins"],"prefix":"10.1038","volume":"17","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-9818-9344","authenticated-orcid":false,"given":"Yuta","family":"Nihongaki","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0198-4465","authenticated-orcid":false,"given":"Hideaki T.","family":"Matsubayashi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7957-7624","authenticated-orcid":false,"given":"Takanari","family":"Inoue","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2021,5,3]]},"reference":[{"key":"791_CR1","doi-asserted-by":"publisher","first-page":"307","DOI":"10.1038\/s41580-020-0214-3","volume":"21","author":"C Janke","year":"2020","unstructured":"Janke, C. & Magiera, M. M. The tubulin code and its role in controlling microtubule properties and functions. Nat. Rev. Mol. Cell Biol. 21, 307\u2013326 (2020).","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"791_CR2","doi-asserted-by":"publisher","first-page":"a022608","DOI":"10.1101\/cshperspect.a022608","volume":"10","author":"HV Goodson","year":"2018","unstructured":"Goodson, H. V. & Jonasson, E. M. Microtubules and microtubule-associated proteins. Cold Spring Harb. Perspect. Biol. 10, a022608 (2018).","journal-title":"Cold Spring Harb. Perspect. Biol."},{"key":"791_CR3","doi-asserted-by":"publisher","first-page":"804","DOI":"10.1016\/j.tcb.2019.07.004","volume":"29","author":"S Bodakuntla","year":"2019","unstructured":"Bodakuntla, S., Jijumon, A. S., Villablanca, C., Gonzalez-Billault, C. & Janke, C. Microtubule-associated proteins: structuring the cytoskeleton. Trends Cell Biol. 29, 804\u2013819 (2019).","journal-title":"Trends Cell Biol."},{"key":"791_CR4","doi-asserted-by":"publisher","first-page":"759","DOI":"10.1083\/jcb.200606074","volume":"174","author":"BK Garvalov","year":"2006","unstructured":"Garvalov, B. K. et al. Luminal particles within cellular microtubules. J. Cell Biol. 174, 759\u2013765 (2006).","journal-title":"J. Cell Biol."},{"key":"791_CR5","doi-asserted-by":"publisher","first-page":"520","DOI":"10.1083\/jcb.99.2.520","volume":"99","author":"PR Burton","year":"1984","unstructured":"Burton, P. R. Luminal material in microtubules of frog olfactory axons: structure and distribution. J. Cell Biol. 99, 520\u2013528 (1984).","journal-title":"J. Cell Biol."},{"key":"791_CR6","doi-asserted-by":"publisher","first-page":"604","DOI":"10.1083\/jcb.39.3.604","volume":"39","author":"A Peters","year":"1968","unstructured":"Peters, A., Proskauer, C. C. & Kaiserman-Abramof, I. R. The small pyramidal neuron of the rat cerebral cortex. J. Cell Biol. 39, 604\u2013619 (1968).","journal-title":"J. Cell Biol."},{"key":"791_CR7","doi-asserted-by":"publisher","first-page":"R1287","DOI":"10.1016\/j.cub.2017.10.044","volume":"27","author":"C Janke","year":"2017","unstructured":"Janke, C. & Montagnac, G. Causes and consequences of microtubule acetylation. Curr. Biol. 27, R1287\u2013R1292 (2017).","journal-title":"Curr. Biol."},{"key":"791_CR8","doi-asserted-by":"publisher","first-page":"328","DOI":"10.1126\/science.aai8764","volume":"356","author":"Z Xu","year":"2017","unstructured":"Xu, Z. et al. Microtubules acquire resistance from mechanical breakage through intralumenal acetylation. Science 356, 328\u2013332 (2017).","journal-title":"Science"},{"key":"791_CR9","doi-asserted-by":"publisher","first-page":"391","DOI":"10.1038\/ncb3481","volume":"19","author":"D Portran","year":"2017","unstructured":"Portran, D., Schaedel, L., Xu, Z., Th\u00e9ry, M. & Nachury, M. V. Tubulin acetylation protects long-lived microtubules against mechanical ageing. Nat. Cell Biol. 19, 391\u2013398 (2017).","journal-title":"Nat. Cell Biol."},{"key":"791_CR10","doi-asserted-by":"publisher","DOI":"10.1038\/s41467-018-04121-y","volume":"9","author":"N Shah","year":"2018","unstructured":"Shah, N. et al. TAK1 activation of \u03b1TAT1 and microtubule hyperacetylation control AKT signaling and cell growth. Nat. Commun. 9, 1696 (2018).","journal-title":"Nat. Commun."},{"key":"791_CR11","doi-asserted-by":"publisher","first-page":"567","DOI":"10.1038\/nature12571","volume":"502","author":"G Montagnac","year":"2013","unstructured":"Montagnac, G. et al. \u03b1TAT1 catalyses microtubule acetylation at clathrin-coated pits. Nature 502, 567\u2013570 (2013).","journal-title":"Nature"},{"key":"791_CR12","doi-asserted-by":"publisher","first-page":"218","DOI":"10.1038\/nature09324","volume":"467","author":"JS Akella","year":"2010","unstructured":"Akella, J. S. et al. MEC-17 is an \u03b1-tubulin acetyltransferase. Nature 467, 218\u2013222 (2010).","journal-title":"Nature"},{"key":"791_CR13","doi-asserted-by":"publisher","first-page":"21517","DOI":"10.1073\/pnas.1013728107","volume":"107","author":"T Shida","year":"2010","unstructured":"Shida, T., Cueva, J. G., Xu, Z., Goodman, M. B. & Nachury, M. V. The major \u03b1-tubulin K40 acetyltransferase TAT1 promotes rapid ciliogenesis and efficient mechanosensation. Proc. Natl Acad. Sci. USA 107, 21517\u201321522 (2010).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"791_CR14","doi-asserted-by":"publisher","first-page":"763","DOI":"10.1016\/j.cellsig.2010.10.014","volume":"23","author":"D Perdiz","year":"2011","unstructured":"Perdiz, D., Mackeh, R., Po\u00fcs, C. & Baillet, A. The ins and outs of tubulin acetylation: more than just a post-translational modification? Cell. Signal. 23, 763\u2013771 (2011).","journal-title":"Cell. Signal."},{"key":"791_CR15","doi-asserted-by":"publisher","first-page":"1405","DOI":"10.1016\/j.cell.2014.03.061","volume":"157","author":"A Szyk","year":"2014","unstructured":"Szyk, A. et al. Molecular basis for age-dependent microtubule acetylation by tubulin acetyltransferase. Cell 157, 1405\u20131415 (2014).","journal-title":"Cell"},{"key":"791_CR16","doi-asserted-by":"publisher","first-page":"E7176","DOI":"10.1073\/pnas.1605397113","volume":"113","author":"C Coombes","year":"2016","unstructured":"Coombes, C. et al. Mechanism of microtubule lumen entry for the \u03b1-tubulin acetyltransferase enzyme \u03b1TAT1. Proc. Natl Acad. Sci. USA 113, E7176\u2013E7184 (2016).","journal-title":"Proc. Natl Acad. Sci. USA"},{"key":"791_CR17","doi-asserted-by":"publisher","DOI":"10.1038\/srep35624","volume":"6","author":"N Ly","year":"2016","unstructured":"Ly, N. et al. TAT1 controls longitudinal spreading of acetylation marks from open microtubules extremities. Sci. Rep. 6, 35624 (2016).","journal-title":"Sci. Rep."},{"key":"791_CR18","doi-asserted-by":"publisher","first-page":"e48204","DOI":"10.1371\/journal.pone.0048204","volume":"7","author":"V Soppina","year":"2012","unstructured":"Soppina, V., Herbstman, J. F., Skiniotis, G. & Verhey, K. J. Luminal localization of \u03b1-tubulin K40 acetylation by cryo-EM analysis of fab-labeled microtubules. PLoS ONE 7, e48204 (2012).","journal-title":"PLoS ONE"},{"key":"791_CR19","doi-asserted-by":"publisher","first-page":"514","DOI":"10.1007\/s002490050161","volume":"27","author":"D Odde","year":"1998","unstructured":"Odde, D. Diffusion inside microtubules. Eur. Biophys. J. 27, 514\u2013520 (1998).","journal-title":"Eur. Biophys. J."},{"key":"791_CR20","first-page":"1245","volume":"6","author":"TA Reid","year":"2017","unstructured":"Reid, T. A., Coombes, C. & Gardner, M. K. Manipulation and quantification of microtubule lattice integrity. Biol. Open 6, 1245\u20131256 (2017).","journal-title":"Biol. Open"},{"key":"791_CR21","doi-asserted-by":"publisher","first-page":"900","DOI":"10.1016\/S0960-9822(95)00180-1","volume":"5","author":"I Arnal","year":"1995","unstructured":"Arnal, I. & Wade, R. H. How does taxol stabilize microtubules? Curr. Biol. 5, 900\u2013908 (1995).","journal-title":"Curr. Biol."},{"key":"791_CR22","doi-asserted-by":"publisher","first-page":"462","DOI":"10.1007\/s00249-003-0386-8","volume":"33","author":"IAT Schaap","year":"2004","unstructured":"Schaap, I. A. T., De Pablo, P. J. & Schmidt, C. F. Resolving the molecular structure of microtubules under physiological conditions with scanning force microscopy. Eur. Biophys. J. 33, 462\u2013467 (2004).","journal-title":"Eur. Biophys. J."},{"key":"791_CR23","doi-asserted-by":"publisher","first-page":"572","DOI":"10.1107\/S2059798318001948","volume":"74","author":"J Atherton","year":"2018","unstructured":"Atherton, J., Stouffer, M., Francis, F. & Moores, C. A. Microtubule architecture in vitro and in cells revealed by cryo-electron tomography. Acta Crystallogr. D Struct. Biol. 74, 572\u2013584 (2018).","journal-title":"Acta Crystallogr. D Struct. Biol."},{"key":"791_CR24","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1007\/s00424-012-1208-6","volume":"465","author":"R DeRose","year":"2013","unstructured":"DeRose, R., Miyamoto, T. & Inoue, T. Manipulating signaling at will: chemically-inducible dimerization (CID) techniques resolve problems in cell biology. Pflug. Arch. 465, 409\u2013417 (2013).","journal-title":"Pflug. Arch."},{"key":"791_CR25","doi-asserted-by":"publisher","first-page":"663","DOI":"10.1016\/j.cbpa.2013.04.027","volume":"17","author":"YC Lin","year":"2013","unstructured":"Lin, Y. C., Phua, S. C., Lin, B. & Inoue, T. Visualizing molecular diffusion through passive permeability barriers in cells: conventional and novel approaches. Curr. Opin. Chem. Biol. 17, 663\u2013671 (2013).","journal-title":"Curr. Opin. Chem. Biol."},{"key":"791_CR26","doi-asserted-by":"publisher","first-page":"1117","DOI":"10.1016\/j.cell.2014.03.053","volume":"157","author":"GM Alushin","year":"2014","unstructured":"Alushin, G. M. et al. High-resolution microtubule structures reveal the structural transitions in \u03b1\u03b2-tubulin upon GTP hydrolysis. Cell 157, 1117\u20131129 (2014).","journal-title":"Cell"},{"key":"791_CR27","doi-asserted-by":"publisher","first-page":"723","DOI":"10.1152\/ajpcell.00462.2010","volume":"300","author":"KW Dunn","year":"2011","unstructured":"Dunn, K. W., Kamocka, M. M. & McDonald, J. H. A practical guide to evaluating colocalization in biological microscopy. Am. J. Physiol. Cell Physiol. 300, 723\u2013742 (2011).","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"791_CR28","doi-asserted-by":"publisher","first-page":"982","DOI":"10.1078\/0171-9335-00129","volume":"79","author":"E Dr\u00e1berov\u00e1","year":"2000","unstructured":"Dr\u00e1berov\u00e1, E., Viklick\u00fd, V. & Dr\u00e1ber, P. Exposure of lumenal microtubule sites after mild fixation. Eur. J. Cell Biol. 79, 982\u2013985 (2000).","journal-title":"Eur. J. Cell Biol."},{"key":"791_CR29","doi-asserted-by":"publisher","first-page":"519","DOI":"10.1242\/jcs.92.3.519","volume":"92","author":"P Dr\u00e1ber","year":"1989","unstructured":"Dr\u00e1ber, P. et al. Differences in the exposure of C- and N-terminal tubulin domains in cytoplasmic microtubules detected with domain-specific monoclonal antibodies. J. Cell Sci. 92, 519\u2013528 (1989).","journal-title":"J. Cell Sci."},{"key":"791_CR30","first-page":"2583","volume":"126","author":"R Ghossoub","year":"2013","unstructured":"Ghossoub, R. et al. Septins 2, 7 and 9 and MAP4 colocalize along the axoneme in the primary cilium and control ciliary length. J. Cell Sci. 126, 2583\u20132594 (2013).","journal-title":"J. Cell Sci."},{"key":"791_CR31","doi-asserted-by":"publisher","first-page":"319","DOI":"10.1016\/0006-291X(76)90524-6","volume":"69","author":"J Hoebeke","year":"1976","unstructured":"Hoebeke, J., Van Nijen, G. & De Brabander, M. Interaction of oncodazole (R 17934), a new anti-tumoral drug, with rat brain tubulin. Biochem. Biophys. Res. Commun. 69, 319\u2013324 (1976).","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"791_CR32","doi-asserted-by":"publisher","first-page":"737","DOI":"10.1016\/j.chembiol.2017.05.016","volume":"24","author":"G S\u00e1ez-Calvo","year":"2017","unstructured":"S\u00e1ez-Calvo, G. et al. Triazolopyrimidines are microtubule-stabilizing agents that bind the vinca inhibitor site of tubulin. Cell Chem. Biol. 24, 737\u2013750 (2017).","journal-title":"Cell Chem. Biol."},{"key":"791_CR33","doi-asserted-by":"publisher","first-page":"2039","DOI":"10.1016\/j.jmb.2015.03.005","volume":"427","author":"KE Miller","year":"2015","unstructured":"Miller, K. E., Kim, Y., Huh, W. K. & Park, H. O. Bimolecular fluorescence complementation (BiFC) analysis: advances and recent applications for genome-wide interaction studies. J. Mol. Biol. 427, 2039\u20132055 (2015).","journal-title":"J. Mol. Biol."},{"key":"791_CR34","doi-asserted-by":"publisher","first-page":"eaaz4344","DOI":"10.1126\/sciadv.aaz4344","volume":"6","author":"C Cuveillier","year":"2020","unstructured":"Cuveillier, C. et al. MAP6 is an intraluminal protein that induces neuronal microtubules to coil. Sci. Adv. 6, eaaz4344 (2020).","journal-title":"Sci. Adv."},{"key":"791_CR35","doi-asserted-by":"publisher","first-page":"437","DOI":"10.1038\/nchembio.1252","volume":"9","author":"YC Lin","year":"2013","unstructured":"Lin, Y. C. et al. Chemically inducible diffusion trap at cilia reveals molecular sieve-like barrier. Nat. Chem. Biol. 9, 437\u2013443 (2013).","journal-title":"Nat. Chem. Biol."},{"key":"791_CR36","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1083\/jcb.201212024","volume":"203","author":"DK Breslow","year":"2013","unstructured":"Breslow, D. K., Koslover, E. F., Seydel, F., Spakowitz, A. J. & Nachury, M. V. An in vitro assay for entry into cilia reveals unique properties of the soluble diffusion barrier. J. Cell Biol. 203, 129\u2013147 (2013).","journal-title":"J. Cell Biol."},{"key":"791_CR37","doi-asserted-by":"publisher","first-page":"4715","DOI":"10.1021\/ja043277y","volume":"127","author":"LA Banaszynski","year":"2005","unstructured":"Banaszynski, L. A., Liu, C. W. & Wandless, T. J. Characterization of the FKBP\u00b7rapamycin\u00b7FRB ternary complex. J. Am. Chem. Soc. 127, 4715\u20134721 (2005).","journal-title":"J. Am. Chem. Soc."},{"key":"791_CR38","doi-asserted-by":"publisher","first-page":"99","DOI":"10.1016\/j.chembiol.2005.10.017","volume":"13","author":"JH Bayle","year":"2006","unstructured":"Bayle, J. H. et al. Rapamycin analogs with differential binding specificity permit orthogonal control of protein activity. Chem. Biol. 13, 99\u2013107 (2006).","journal-title":"Chem. Biol."},{"key":"791_CR39","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1091\/mbc.e13-07-0387","volume":"25","author":"SC Howes","year":"2014","unstructured":"Howes, S. C., Alushin, G. M., Shida, T., Nachury, M. V. & Nogales, E. Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure. Mol. Biol. Cell 25, 257\u2013266 (2014).","journal-title":"Mol. Biol. Cell"},{"key":"791_CR40","doi-asserted-by":"publisher","first-page":"909","DOI":"10.1016\/j.cell.2019.09.030","volume":"179","author":"M Ma","year":"2019","unstructured":"Ma, M. et al. Structure of the decorated ciliary doublet microtubule. Cell 179, 909\u2013922 (2019).","journal-title":"Cell"},{"key":"791_CR41","doi-asserted-by":"publisher","first-page":"455","DOI":"10.1038\/417455a","volume":"417","author":"C Hubbert","year":"2002","unstructured":"Hubbert, C. et al. HDAC6 is a microtubule-associated deacetylase. Nature 417, 455\u2013458 (2002).","journal-title":"Nature"}],"container-title":["Nature Chemical Biology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41589-021-00791-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41589-021-00791-w","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41589-021-00791-w.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,2,1]],"date-time":"2023-02-01T02:29:08Z","timestamp":1675218548000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41589-021-00791-w"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,5,3]]},"references-count":41,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2021,8]]}},"alternative-id":["791"],"URL":"https:\/\/doi.org\/10.1038\/s41589-021-00791-w","relation":{},"ISSN":["1552-4450","1552-4469"],"issn-type":[{"value":"1552-4450","type":"print"},{"value":"1552-4469","type":"electronic"}],"subject":[],"published":{"date-parts":[[2021,5,3]]},"assertion":[{"value":"25 July 2020","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"30 March 2021","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"3 May 2021","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}]}}