Roll-Mecak, A. The tubulin code in microtubule dynamics and information encoding. Dev. Cell 54, 7–20 (2020).

Article  CAS  PubMed  Google Scholar 

Bieling, P. et al. CLIP-170 tracks growing microtubule ends by dynamically recognizing composite EB1/tubulin-binding sites. J. Cell Biol. 183, 1223–1233 (2008).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Chen, J. et al. α-Tubulin tail modifications regulate microtubule stability through selective effector recruitment, not changes in intrinsic polymer dynamics. Dev. Cell 56, 2016–2028 (2021).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Hotta, T. et al. EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules. Curr. Biol. 32, 3898–3910 (2022).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Gundersen, G. G. & Bulinski, J. C. Selective stabilization of microtubules oriented toward the direction of cell migration. Proc. Natl Acad. Sci. USA 85, 5946–5950 (1988).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Gurland, G. & Gundersen, G. G. Stable, detyrosinated microtubules function to localize vimentin intermediate filaments in fibroblasts. J. Cell Biol. 131, 1275–1290 (1995).

Article  CAS  PubMed  Google Scholar 

Kerr, J. P. et al. Detyrosinated microtubules modulate mechanotransduction in heart and skeletal muscle. Nat. Commun. 6, 8526 (2015).

Article  CAS  PubMed  Google Scholar 

Palazzo, A. F., Eng, C. H., Schlaepfer, D. D., Marcantonio, E. E. & Gundersen, G. G. Localized stabilization of microtubules by integrin- and FAK-facilitated ρ signaling. Science 303, 836–839 (2004).

Article  CAS  PubMed  Google Scholar 

Robison, P. et al. Detyrosinated microtubules buckle and bear load in contracting cardiomyocytes. Science 352, aaf0659 (2016).

Article  PubMed  PubMed Central  Google Scholar 

Lacroix, B. et al. Tubulin polyglutamylation stimulates spastin-mediated microtubule severing. J. Cell Biol. 189, 945–954 (2010).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Sharma, N. et al. Katanin regulates dynamics of microtubules and biogenesis of motile cilia. J. Cell Biol. 178, 1065–1079 (2007).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Szczesna, E. et al. Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing. Dev. Cell 57, 2497–2513 (2022).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Valenstein, M. L. & Roll-Mecak, A. Graded control of microtubule severing by tubulin glutamylation. Cell 164, 911–921 (2016).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Barisic, M. et al. Mitosis. Microtubule detyrosination guides chromosomes during mitosis. Science 348, 799–803 (2015).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Lessard, D. V. et al. Polyglutamylation of tubulin’s C-terminal tail controls pausing and motility of kinesin-3 family member KIF1A. J. Biol. Chem. 294, 6353–6363 (2019).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Sirajuddin, M., Rice, L. M. & Vale, R. D. Regulation of microtubule motors by tubulin isotypes and post-translational modifications. Nat. Cell Biol. 16, 335–344 (2014).

Article  CAS  PubMed  PubMed Central  Google Scholar 

McKenney, R. J., Huynh, W., Vale, R. D. & Sirajuddin, M. Tyrosination of α-tubulin controls the initiation of processive dynein-dynactin motility. EMBO J. 35, 1175–1185 (2016).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Nirschl, J. J., Magiera, M. M., Lazarus, J. E., Janke, C. & Holzbaur, E. L. α-Tubulin tyrosination and CLIP-170 phosphorylation regulate the initiation of dynein-driven transport in neurons. Cell Rep. 14, 2637–2652 (2016).

Article  CAS  PubMed  PubMed Central  Google Scholar 

van Dijk, J. et al. A targeted multienzyme mechanism for selective microtubule polyglutamylation. Mol. Cell 26, 437–448 (2007).

Article  PubMed  Google Scholar 

Garnham, C. P. & Roll-Mecak, A. The chemical complexity of cellular microtubules: tubulin post-translational modification enzymes and their roles in tuning microtubule functions. Cytoskeleton (Hoboken) 69, 442–463 (2012).

Article  CAS  PubMed  Google Scholar 

Gundersen, G. G., Khawaja, S. & Bulinski, J. C. Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiation. J. Cell Biol. 109, 2275–2288 (1989).

Article  CAS  PubMed  Google Scholar 

Bodakuntla, S. et al. Tubulin polyglutamylation is a general traffic control mechanism in hippocampal neurons. J. Cell Sci. 133, jcs241802 (2020).

Article  CAS  PubMed  Google Scholar 

Magiera, M. M., Singh, P., Gadadhar, S. & Janke, C. Tubulin posttranslational modifications and emerging links to human disease. Cell 173, 1323–1327 (2018).

Article  CAS  PubMed  Google Scholar 

Karakaya, M. et al. Biallelic variant in AGTPBP1 causes infantile lower motor neuron degeneration and cerebellar atrophy. Am. J. Med. Genet. A 179, 1580–1584 (2019).

Article  CAS  PubMed  Google Scholar 

Maddirevula, S. et al. Autozygome and high throughput confirmation of disease genes candidacy. Genet. Med. 21, 736–742 (2019).

Article  CAS  PubMed  Google Scholar 

Shashi, V. et al. Loss of tubulin deglutamylase CCP1 causes infantile-onset neurodegeneration. EMBO J. 37, e100540 (2018).

Article  PubMed  PubMed Central  Google Scholar 

Sheffer, R. et al. Biallelic variants in AGTPBP1, involved in tubulin deglutamylation, are associated with cerebellar degeneration and motor neuropathy. Eur. J. Hum. Genet. 27, 1419–1426 (2019).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Konno, A. et al. TTLL9−/− mice sperm flagella show shortening of doublet 7, reduction of doublet 5 polyglutamylation and a stall in beating. J. Cell Sci. 129, 2757–2766 (2016).

CAS  PubMed  Google Scholar 

Pathak, N., Austin, C. A. & Drummond, I. A. Tubulin tyrosine ligase-like genes TTLL3 and TTLL6 maintain zebrafish cilia structure and motility. J. Biol. Chem. 286, 11685–11695 (2011).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Bosch Grau, M. et al. Tubulin glycylases and glutamylases have distinct functions in stabilization and motility of ependymal cilia. J. Cell Biol. 202, 441–451 (2013).

Article  PubMed  PubMed Central  Google Scholar 

Ikegami, K., Sato, S., Nakamura, K., Ostrowski, L. E. & Setou, M. Tubulin polyglutamylation is essential for airway ciliary function through the regulation of beating asymmetry. Proc. Natl Acad. Sci. USA 107, 10490–10495 (2010).

Article  CAS  PubMed  PubMed Central  Google Scholar 

He, K. et al. Axoneme polyglutamylation regulated by Joubert syndrome protein ARL13B controls ciliary targeting of signaling molecules. Nat. Commun. 9, 3310 (2018).

Article  PubMed  PubMed Central  Google Scholar 

Hong, S. R. et al. Spatiotemporal manipulation of ciliary glutamylation reveals its roles in intraciliary trafficking and Hedgehog signaling. Nat. Commun. 9, 1732 (2018).

Article  PubMed  PubMed Central  Google Scholar 

Kubo, T. et al. A conserved flagella-associated protein in Chlamydomonas, FAP234, is essential for axonemal localization of tubulin polyglutamylase TTLL9. Mol. Biol. Cell 25, 107–117 (2014).

Article  PubMed  PubMed Central  Google Scholar 

Lee, J. E. et al. CEP41 is mutated in Joubert syndrome and is required for tubulin glutamylation at the cilium. Nat. Genet. 44, 193–199 (2012).

Article  CAS  PubMed  PubMed Central  Google Scholar 

Bompard, G. et al. CSAP acts as a regulator of TTLL-mediated microtubule glutamylation. Cell Rep. 25, 2866–2877 (2018).

Article