Posttranslational Modifications of Tubulin and Cilia

Lysine acetylation targets protein complexes and co-regulates major cellular functions

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HDAC6 is a microtubule-associated deacetylase

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The Human Sir2 Ortholog, SIRT2, Is an NAD+-Dependent Tubulin Deacetylase

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High-Resolution Model of the Microtubule

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Microtubule Acetylation Promotes Kinesin-1 Binding and Transport

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HEF1-Dependent Aurora A Activation Induces Disassembly of the Primary Cilium

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Monoclonal antibodies specific for an acetylated form of alpha-tubulin recognize the antigen in cilia and flagella from a variety of organisms.

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HDAC-6 interacts with and deacetylates tubulin and microtubules in vivo

Zhang, Y., Li, N., Caron, C., Matthias, G., Hess, D., Khochbin, S., & Matthias, P. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg115 · Cited by 740 · see citing works

Regulation of microtubule motors by tubulin isotypes and post-translational modifications

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The Chlamydomonas kinesin-like protein FLA10 is involved in motility associated with the flagellar membrane.

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Mice Lacking Histone Deacetylase 6 Have Hyperacetylated Tubulin but Are Viable and Develop Normally

Zhang, Y., Kwon, S., Yamaguchi, T., Cubizolles, F., Rousseaux, S., Kneissel, M., Cao, C., Li, N., Cheng, H.-L., Chua, K., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01154-06 · Cited by 559 · cited 1× · see citing works

The Tubulin Code

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Posttranslational Glutamylation of α-tubulin

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Functional genomic screen for modulators of ciliogenesis and cilium length

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The tubulin code: Molecular components, readout mechanisms, and functions

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MEC-17 is an α-tubulin acetyltransferase

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The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation

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

A Family of Protein-Deglutamylating Enzymes Associated with Neurodegeneration

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Post-translational modifications of tubulin: pathways to functional diversity of microtubules

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Genetic control of differentiation of the Caenorhabditis elegans touch receptor neurons.

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Tubulin Polyglutamylase Enzymes Are Members of the TTL Domain Protein Family

Janke, C., Rogowski, K., Włoga, D., et al. (2005) · Science · doi:10.1126/science.1113010 · Cited by 376 · see citing works

Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin

Roll‐Mecak, A., & Vale, R. D. (2008) · Nature · doi:10.1038/nature06482 · Cited by 340 · see citing works

A Targeted Multienzyme Mechanism for Selective Microtubule Polyglutamylation

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Identification of an acetylation site of Chlamydomonas alpha-tubulin.

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Tubulin polyglutamylation stimulates spastin-mediated microtubule severing

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Polyglycylation of Tubulin: a Posttranslational Modification in Axonemal Microtubules

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A vital role of tubulin-tyrosine-ligase for neuronal organization

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Paralyzed flagella mutants of Chlamydomonas reinhardtii. Defective for axonemal doublet microtubule arms.

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Graded Control of Microtubule Severing by Tubulin Glutamylation

Valenstein, M. L., & Roll‐Mecak, A. (2016) · Cell · doi:10.1016/j.cell.2016.01.019 · Cited by 268 · see citing works

Chlamydomonas alpha-tubulin is posttranslationally modified in the flagella during flagellar assembly.

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Microtubule doublets are double-track railways for intraflagellar transport trains

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Purkinje cell degeneration ( pcd ) Phenotypes Caused by Mutations in the Axotomy-Induced Gene, Nna1

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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

Structural basis of tubulin tyrosination by tubulin tyrosine ligase

Prota, A. E., Magiera, M. M., Kuijpers, M., Bargsten, K., FREY, D. J., Wieser, M. M., Jaussi, R., Hoogenraad, C. C., Kammerer, R. A., Janke, C., et al. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201211017 · 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

Characterization of the tubulin-tyrosine ligase.

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Functional analysis of an individual IFT protein: IFT46 is required for transport of outer dynein arms into flagella

Hou, Y., Qin, H., Follit, J. A., Pazour, G. J., Rosenbaum, J. L., & Witman, G. B. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200608041 · Cited by 226 · see citing works

Glutamylation of the DNA sensor cGAS regulates its binding and synthase activity in antiviral immunity

Xia, P., Ye, B., Wang, S., Zhu, X., Du, Y., Xiong, Z., Tian, Y., & Fan, Z. (2016) · Nature Immunology · doi:10.1038/ni.3356 · Cited by 220 · 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

Functional diversity of axonemal dyneins as studied in Chlamydomonas mutants

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Electron-tomographic analysis of intraflagellar transport particle trains in situ

Pigino, G., Geimer, S., Lanzavecchia, S., Paccagnini, E., Cantele, F., Diener, D. R., Rosenbaum, J. L., & Lupetti, P. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200905103 · Cited by 204 · see citing works

Accumulation of delta 2-tubulin, a major tubulin variant that cannot be tyrosinated, in neuronal tissues and in stable microtubule assemblies

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Tubulin Polyglutamylation Regulates Axonemal Motility by Modulating Activities of Inner-Arm Dyneins

Kubo, T., Yanagisawa, H., Yagi, T., Hirono, M., & Kamiya, R. (2010) · Current Biology · doi:10.1016/j.cub.2009.12.058 · Cited by 194 · see citing works

Evolutionary Divergence of Enzymatic Mechanisms for Posttranslational Polyglycylation

Rogowski, K., Juge, F., van Dijk, J., Włoga, D., Strub, J., Levilliers, N., Thomas, D., Bré, M., DORSSELAER, A. V., Gaertig, J., et al. (2009) · Cell · doi:10.1016/j.cell.2009.05.020 · Cited by 190 · see citing works

TTLL3 Is a Tubulin Glycine Ligase that Regulates the Assembly of Cilia

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CEP41 is mutated in Joubert syndrome and is required for tubulin glutamylation at the cilium

Lee, J. E., Silhavy, J. L., Zaki, M. S., Schroth, J., Bielas, S. L., Marsh, S., Olvera, J., Brancati, F., Iannicelli, M., Ikegami, K., et al. (2012) · Nature Genetics · doi:10.1038/ng.1078 · Cited by 184 · see citing works

Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure

Howes, S. C., Alushin, G. M., Shida, T., Nachury, M. V., & Nogales, E. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-07-0387 · Cited by 183 · see citing works

Preferential action of a brain detyrosinolating carboxypeptidase on polymerized tubulin.

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Writing and Reading the Tubulin Code

Yu, I., Garnham, C. P., & Roll‐Mecak, A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.637447 · Cited by 180 · see citing works

Posttranslational Acetylation of α-Tubulin Constrains Protofilament Number in Native Microtubules

Cueva, J. G., Hsin, J., Huang, K. C., & Goodman, M. B. (2012) · Current Biology · doi:10.1016/j.cub.2012.05.012 · Cited by 178 · see citing works

Lineage specificity of primary cilia in the mouse embryo

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Tubulin polyglutamylation is essential for airway ciliary function through the regulation of beating asymmetry

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Tubulin Glutamylation Regulates Ciliary Motility by Altering Inner Dynein Arm Activity

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MEC-12, an α-tubulin required for touch sensitivity in C. elegans

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Deacetylation of α-tubulin and cortactin is required for HDAC6 to trigger ciliary disassembly

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Katanin regulates dynamics of microtubules and biogenesis of motile cilia

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Genetically Separable Functions of the MEC-17 Tubulin Acetyltransferase Affect Microtubule Organization

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Axonemal tubulin polyglycylation probed with two monoclonal antibodies: widespread evolutionary distribution, appearance during spermatozoan maturation and possible function in motility

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Structure of tubulin C‐terminal domain obtained by subtilisin treatment The major α and β tubulin isotypes from pig brain are glutamylated

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Cryo-electron tomography reveals conserved features of doublet microtubules in flagella

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Mice Lacking α-Tubulin Acetyltransferase 1 Are Viable but Display α-Tubulin Acetylation Deficiency and Dentate Gyrus Distortion

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The light chain p28 associates with a subset of inner dynein arm heavy chains in Chlamydomonas axonemes.

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High level expression of nonacetylatable α‐tubulin in Chlamydomonas reinhardtii

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Polyglycylation of Tubulin Is Essential and Affects Cell Motility and Division in Tetrahymena thermophila

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Tubulin tyrosine ligase structure reveals adaptation of an ancient fold to bind and modify tubulin

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Acetylation of lysine 40 in alpha-tubulin is not essential in Tetrahymena thermophila.

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A novel acetylation of β-tubulin by San modulates microtubule polymerization via down-regulating tubulin incorporation

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Identification of Tubulin Deglutamylase among Caenorhabditis elegans and Mammalian Cytosolic Carboxypeptidases (CCPs)

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Asymmetry of inner dynein arms and inter-doublet links in Chlamydomonas flagella

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Effects of α-Tubulin K40 Acetylation and Detyrosination on Kinesin-1 Motility in a Purified System

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Polyglycylation domain of β-tubulin maintains axonemal architecture and affects cytokinesis in Tetrahymena

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The Tubulin Deglutamylase CCPP-1 Regulates the Function and Stability of Sensory Cilia in C. elegans

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The ubiquitin conjugation system is involved in the disassembly of cilia and flagella

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Tubulin Tyrosine Ligase-like Genes ttll3 and ttll6 Maintain Zebrafish Cilia Structure and Motility

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Tubulin glycylases and glutamylases have distinct functions in stabilization and motility of ependymal cilia

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Mitral cell degeneration and sensory function in the neurological mutant mouse Purkinje cell degeneration (PCD)

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Polyglutamylation Is a Post-translational Modification with a Broad Range of Substrates

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Tetrahymena thermophila contains a conventional γ-tubulin that is differentially required for the maintenance of different microtubule-organizing centers

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Intrinsically disordered tubulin tails: complex tuners of microtubule functions?

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Loss of RPGR glutamylation underlies the pathogenic mechanism of retinal dystrophy caused by TTLL5 mutations

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Luminal Localization of α-tubulin K40 Acetylation by Cryo-EM Analysis of Fab-Labeled Microtubules

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Multivalent Microtubule Recognition by Tubulin Tyrosine Ligase-like Family Glutamylases

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CYLD mediates ciliogenesis in multiple organs by deubiquitinating Cep70 and inactivating HDAC6

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Tubulin glycylases are required for primary cilia, control of cell proliferation and tumor development in colon

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Glutamylation on α-Tubulin Is Not Essential but Affects the Assembly and Functions of a Subset of Microtubules in Tetrahymena thermophila

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Mechanism of ciliary disassembly

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Relationship between microtubule dynamics and lamellipodium formation revealed by direct imaging of microtubules in cells treated with nocodazole or taxol

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Tubulin Acetyltransferase αTAT1 Destabilizes Microtubules Independently of Its Acetylation Activity

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