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  1. Article ; Online: Glutamylation is a negative regulator of microtubule growth.

    Chen, Jiayi / Roll-Mecak, Antonina

    Molecular biology of the cell

    2023  Volume 34, Issue 7, Page(s) ar70

    Abstract: Microtubules are noncovalent polymers built from αβ-tubulin dimers. The disordered C-terminal tubulin tails are functionalized with multiple glutamate chains of variable lengths added and removed by tubulin tyrosine ligases (TTLLs) and carboxypeptidases ( ...

    Abstract Microtubules are noncovalent polymers built from αβ-tubulin dimers. The disordered C-terminal tubulin tails are functionalized with multiple glutamate chains of variable lengths added and removed by tubulin tyrosine ligases (TTLLs) and carboxypeptidases (CCPs). Glutamylation is abundant on stable microtubule arrays such as in axonemes and axons, and its dysregulation leads to human pathologies. Despite this, the effects of glutamylation on intrinsic microtubule dynamics are unclear. Here we generate tubulin with short and long glutamate chains and show that glutamylation slows the rate of microtubule growth and increases catastrophes as a function of glutamylation levels. This implies that the higher stability of glutamylated microtubules in cells is due to effectors. Interestingly, EB1 is minimally affected by glutamylation and thus can report on the growth rates of both unmodified and glutamylated microtubules. Finally, we show that glutamate removal by CCP1 and 5 is synergistic and occurs preferentially on soluble tubulin, unlike TTLL enzymes that prefer microtubules. This substrate preference establishes an asymmetry whereby once the microtubule depolymerizes, the released tubulin is reset to a less-modified state, while polymerized tubulin accumulates the glutamylation mark. Our work shows that a modification on the disordered tubulin tails can directly affect microtubule dynamics and furthers our understanding of the mechanistic underpinnings of the tubulin code.
    MeSH term(s) Humans ; Tubulin/metabolism ; Microtubules/metabolism ; Glutamic Acid/metabolism ; Axoneme/metabolism ; Protein Processing, Post-Translational
    Chemical Substances Tubulin ; Glutamic Acid (3KX376GY7L)
    Language English
    Publishing date 2023-04-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E23-01-0030
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    Zs.A 2853: Show issues Location:
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    Zs.MO 410: Show issues

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  2. Article ; Online: Editorial overview: Microtubules in nervous system development.

    Bradke, Frank / Roll-Mecak, Antonina

    Developmental neurobiology

    2021  Volume 81, Issue 3, Page(s) 229–230

    MeSH term(s) Microtubules ; Nervous System ; Organogenesis
    Language English
    Publishing date 2021-04-17
    Publishing country United States
    Document type Editorial ; Research Support, N.I.H., Intramural
    ZDB-ID 2256184-5
    ISSN 1932-846X ; 1097-4695 ; 1932-8451 ; 0022-3034
    ISSN (online) 1932-846X ; 1097-4695
    ISSN 1932-8451 ; 0022-3034
    DOI 10.1002/dneu.22817
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  3. Article ; Online: The Tubulin Code in Microtubule Dynamics and Information Encoding.

    Roll-Mecak, Antonina

    Developmental cell

    2020  Volume 54, Issue 1, Page(s) 7–20

    Abstract: Microtubules are non-covalent mesoscale polymers central to the eukaryotic cytoskeleton. Microtubule structure, dynamics, and mechanics are modulated by a cell's choice of tubulin isoforms and post-translational modifications, a "tubulin code," which is ... ...

    Abstract Microtubules are non-covalent mesoscale polymers central to the eukaryotic cytoskeleton. Microtubule structure, dynamics, and mechanics are modulated by a cell's choice of tubulin isoforms and post-translational modifications, a "tubulin code," which is thought to support the diverse morphology and dynamics of microtubule arrays across various cell types, cell cycle, and developmental stages. We give a brief historical overview of research into tubulin diversity and highlight recent progress toward uncovering the mechanistic underpinnings of the tubulin code. As a large number of essential pathways converge upon the microtubule cytoskeleton, understanding how cells utilize tubulin diversity is crucial to understanding cellular physiology and disease.
    MeSH term(s) Animals ; Humans ; Microtubule-Associated Proteins/chemistry ; Microtubule-Associated Proteins/metabolism ; Microtubules/chemistry ; Microtubules/metabolism ; Molecular Dynamics Simulation ; Protein Processing, Post-Translational ; Tubulin/chemistry ; Tubulin/genetics ; Tubulin/metabolism
    Chemical Substances Microtubule-Associated Proteins ; Tubulin
    Language English
    Publishing date 2020-07-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/j.devcel.2020.06.008
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    Zs.A 5742: Show issues Location:
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    Zs.MG 76: Show issues

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  4. Article ; Online: A look under the hood of the machine that makes cilia beat.

    Zehr, Elena A / Roll-Mecak, Antonina

    Nature structural & molecular biology

    2022  Volume 29, Issue 5, Page(s) 416–418

    Language English
    Publishing date 2022-05-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-022-00778-8
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    Zs.MG 56: Show issues

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  5. Article ; Online: A Microtubule-Myelination Connection.

    Roll-Mecak, Antonina

    Cell

    2019  Volume 179, Issue 1, Page(s) 54–56

    Abstract: Microtubules are critical for the extension of oligodendrocyte processes and myelin deposition, yet our knowledge of their microtubule biogenesis is limited. In this issue of Cell, Fu et al. (2019) identify an oligodendrocyte-enriched microtubule ... ...

    Abstract Microtubules are critical for the extension of oligodendrocyte processes and myelin deposition, yet our knowledge of their microtubule biogenesis is limited. In this issue of Cell, Fu et al. (2019) identify an oligodendrocyte-enriched microtubule regulator that promotes microtubule growth from Golgi outposts and controls myelin sheath elongation, linking microtubule cytoarchitecture and myelination in the CNS.
    MeSH term(s) Microtubules ; Myelin Sheath ; Oligodendroglia
    Language English
    Publishing date 2019-09-12
    Publishing country United States
    Document type Journal Article ; Comment
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2019.08.046
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    Zs.MG 58: Show issues

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  6. Article ; Online: Microtubule-severing enzymes.

    Sarbanes, Stephanie L / Zehr, Elena A / Roll-Mecak, Antonina

    Current biology : CB

    2022  Volume 32, Issue 19, Page(s) R992–R997

    Abstract: Stephanie Sarbanes et al. discuss microtubule-severing enzymes, highlighting their shared structure and mechanism and the diversity of processes in which they participate. ...

    Abstract Stephanie Sarbanes et al. discuss microtubule-severing enzymes, highlighting their shared structure and mechanism and the diversity of processes in which they participate.
    MeSH term(s) Katanin/metabolism ; Microtubules/metabolism
    Chemical Substances Katanin (EC 5.6.1.1)
    Language English
    Publishing date 2022-10-11
    Publishing country England
    Document type Journal Article
    ZDB-ID 1071731-6
    ISSN 1879-0445 ; 0960-9822
    ISSN (online) 1879-0445
    ISSN 0960-9822
    DOI 10.1016/j.cub.2022.08.046
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    Zs.A 3208: Show issues Location:
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  7. Article ; Online: How cells exploit tubulin diversity to build functional cellular microtubule mosaics.

    Roll-Mecak, Antonina

    Current opinion in cell biology

    2018  Volume 56, Page(s) 102–108

    Abstract: Cellular microtubules are mosaic polymers assembled from multiple αβ-tubulin isoforms bearing chemically diverse posttranslational modifications. This tubulin diversity constitutes a combinatorial code that regulates microtubule interactions with ... ...

    Abstract Cellular microtubules are mosaic polymers assembled from multiple αβ-tubulin isoforms bearing chemically diverse posttranslational modifications. This tubulin diversity constitutes a combinatorial code that regulates microtubule interactions with cellular effectors and alters their intrinsic dynamic and mechanical properties. Cells generate stereotyped and complex tubulin modification patterns that are important for their specialized functions. Here we give a brief overview of the tubulin genetic and chemical diversity and highlight recent advances in our understanding of how the tubulin code regulates essential biological processes ranging from intracellular cargo transport, to cell division and cardiomyocyte contraction. Finally, we speculate on the molecular mechanisms for the generation and maintenance of the complex stereotyped modification patterns that form cellular microtubule mosaics.
    MeSH term(s) Animals ; Biological Transport ; Cytoskeleton/metabolism ; Humans ; Microtubules/metabolism ; Protein Isoforms/chemistry ; Protein Isoforms/genetics ; Protein Isoforms/metabolism ; Protein Processing, Post-Translational ; Tubulin/chemistry ; Tubulin/genetics ; Tubulin/metabolism
    Chemical Substances Protein Isoforms ; Tubulin
    Language English
    Publishing date 2018-11-20
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Intramural ; Review
    ZDB-ID 1026381-0
    ISSN 1879-0410 ; 0955-0674
    ISSN (online) 1879-0410
    ISSN 0955-0674
    DOI 10.1016/j.ceb.2018.10.009
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  8. Article ; Online: Watching microtubules grow one tubulin at a time.

    Gudimchuk, Nikita / Roll-Mecak, Antonina

    Proceedings of the National Academy of Sciences of the United States of America

    2019  Volume 116, Issue 15, Page(s) 7163–7165

    MeSH term(s) Biophysical Phenomena ; Microtubules ; Polymers ; Tubulin
    Chemical Substances Polymers ; Tubulin
    Language English
    Publishing date 2019-03-25
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1902991116
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  9. Article ; Online: Phosphinic acid-based inhibitors of tubulin polyglycylation.

    Zhuang, Zaile / Cummings, Steven W / Roll-Mecak, Antonina / Tanner, Martin E

    Chemical communications (Cambridge, England)

    2022  Volume 58, Issue 45, Page(s) 6530–6533

    Abstract: Tubulin polyglycylation is a posttranslational modification that occurs primarily on the axonemes of flagella and cilia and has been shown to be essential for proper sperm motility. Inhibitors of both the initiase and elongase ligases (TTLL8 and TTLL10) ... ...

    Abstract Tubulin polyglycylation is a posttranslational modification that occurs primarily on the axonemes of flagella and cilia and has been shown to be essential for proper sperm motility. Inhibitors of both the initiase and elongase ligases (TTLL8 and TTLL10) are shown to inhibit tubulin glycylation in the low micromolar range.
    MeSH term(s) Cilia/metabolism ; Humans ; Male ; Microtubules/metabolism ; Phosphinic Acids ; Protein Processing, Post-Translational ; Sperm Motility ; Tubulin/metabolism
    Chemical Substances Phosphinic Acids ; Tubulin
    Language English
    Publishing date 2022-06-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 1472881-3
    ISSN 1364-548X ; 1359-7345 ; 0009-241X
    ISSN (online) 1364-548X
    ISSN 1359-7345 ; 0009-241X
    DOI 10.1039/d2cc01783k
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  10. Article ; Online: Structural basis for α-tubulin-specific and modification state-dependent glutamylation.

    Mahalingan, Kishore K / Grotjahn, Danielle A / Li, Yan / Lander, Gabriel C / Zehr, Elena A / Roll-Mecak, Antonina

    Nature chemical biology

    2024  

    Abstract: Microtubules have spatiotemporally complex posttranslational modification patterns. Tubulin tyrosine ligase-like (TTLL) enzymes introduce the most prevalent modifications on α-tubulin and β-tubulin. How TTLLs specialize for specific substrate recognition ...

    Abstract Microtubules have spatiotemporally complex posttranslational modification patterns. Tubulin tyrosine ligase-like (TTLL) enzymes introduce the most prevalent modifications on α-tubulin and β-tubulin. How TTLLs specialize for specific substrate recognition and ultimately modification-pattern generation is largely unknown. TTLL6, a glutamylase implicated in ciliopathies, preferentially modifies tubulin α-tails in microtubules. Cryo-electron microscopy, kinetic analysis and single-molecule biochemistry reveal an unprecedented quadrivalent recognition that ensures simultaneous readout of microtubule geometry and posttranslational modification status. By binding to a β-tubulin subunit, TTLL6 modifies the α-tail of the longitudinally adjacent tubulin dimer. Spanning two tubulin dimers along and across protofilaments (PFs) ensures fidelity of recognition of both the α-tail and the microtubule. Moreover, TTLL6 reads out and is stimulated by glutamylation of the β-tail of the laterally adjacent tubulin dimer, mediating crosstalk between α-tail and β-tail. This positive feedback loop can generate localized microtubule glutamylation patterns. Our work uncovers general principles that generate tubulin chemical and topographic complexity.
    Language English
    Publishing date 2024-04-24
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2202962-X
    ISSN 1552-4469 ; 1552-4450
    ISSN (online) 1552-4469
    ISSN 1552-4450
    DOI 10.1038/s41589-024-01599-0
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    Zs.MG 90: Show issues

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