Tubulin polyglutamylation differentially regulates
microtubule-interacting proteins

J 2023

Tubulin polyglutamylation differentially regulates microtubule-interacting proteins

GENOVA, Mariya; Lenka GRYCOVA; Verena PUTTRICH; Maria M MAGIERA; Zdenek LANSKY et al.

Základní údaje

Originální název

Tubulin polyglutamylation differentially regulates microtubule-interacting proteins

Autoři

GENOVA, Mariya; Lenka GRYCOVA; Verena PUTTRICH; Maria M MAGIERA; Zdenek LANSKY; Carsten JANKE a Marcus BRAUN

Vydání

EMBO Journal, Hoboken (USA), WILEY-BLACKWELL, 2023, 0261-4189

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 9.500

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:90127/23:00139189

Organizační jednotka

CIISB II

Klíčová slova anglicky

katanin; kinesin-1; microtubule-associated Tau; microtubules; polyglutamylation; tubulin posttranslational modifications

Štítky

ne MU, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 3. 2025 09:38, Mgr. Eva Dubská

Anotace

V originále

Tubulin posttranslational modifications have been predicted to control cytoskeletal functions by coordinating the molecular interactions between microtubules and their associating proteins. A prominent tubulin modification in neurons is polyglutamylation, the deregulation of which causes neurodegeneration. Yet, the underlying molecular mechanisms have remained elusive. Here, using in-vitro reconstitution, we determine how polyglutamylation generated by the two predominant neuronal polyglutamylases, TTLL1 and TTLL7, specifically modulates the activities of three major microtubule interactors: the microtubule-associated protein Tau, the microtubule-severing enzyme katanin and the molecular motor kinesin-1. We demonstrate that the unique modification patterns generated by TTLL1 and TTLL7 differentially impact those three effector proteins, thus allowing for their selective regulation. Given that our experiments were performed with brain tubulin from mouse models in which physiological levels and patterns of polyglutamylation were altered by the genetic knockout of the main modifying enzymes, our quantitative measurements provide direct mechanistic insight into how polyglutamylation could selectively control microtubule interactions in neurons.

Návaznosti

90127, velká výzkumná infrastruktura

Název: CIISB II

Citovat

GENOVA, Mariya; Lenka GRYCOVA; Verena PUTTRICH; Maria M MAGIERA; Zdenek LANSKY; Carsten JANKE a Marcus BRAUN. Tubulin polyglutamylation differentially regulates microtubule-interacting proteins. EMBO Journal. Hoboken (USA): WILEY-BLACKWELL, 2023, roč. 42, č. 5, s. 1-17. ISSN 0261-4189. Dostupné z: https://doi.org/10.15252/embj.2022112101.

@article{2487187,
   author = {Genova, Mariya and Grycova, Lenka and Puttrich, Verena and Magiera, Maria M and Lansky, Zdenek and Janke, Carsten and Braun, Marcus},
   article_location = {Hoboken (USA)},
   article_number = {5},
   doi = {https://doi.org/10.15252/embj.2022112101},
   keywords = {katanin; kinesin-1; microtubule-associated Tau; microtubules; polyglutamylation; tubulin posttranslational modifications},
   language = {eng},
   issn = {0261-4189},
   journal = {EMBO Journal},
   title = {Tubulin polyglutamylation differentially regulates microtubule-interacting proteins},
   url = {https://www.embopress.org/doi/full/10.15252/embj.2022112101},
   volume = {42},
   year = {2023}
}

TY  - JOUR
ID  - 2487187
AU  - Genova, Mariya - Grycova, Lenka - Puttrich, Verena - Magiera, Maria M - Lansky, Zdenek - Janke, Carsten - Braun, Marcus
PY  - 2023
TI  - Tubulin polyglutamylation differentially regulates microtubule-interacting proteins
JF  - EMBO Journal
VL  - 42
IS  - 5
SP  - 1-17
EP  - 1-17
PB  - WILEY-BLACKWELL
SN  - 02614189
KW  - katanin
KW  - kinesin-1
KW  - microtubule-associated Tau
KW  - microtubules
KW  - polyglutamylation
KW  - tubulin posttranslational modifications
UR  - https://www.embopress.org/doi/full/10.15252/embj.2022112101
N2  - Tubulin posttranslational modifications have been predicted to control cytoskeletal functions by coordinating the molecular interactions between microtubules and their associating proteins. A prominent tubulin modification in neurons is polyglutamylation, the deregulation of which causes neurodegeneration. Yet, the underlying molecular mechanisms have remained elusive. Here, using in-vitro reconstitution, we determine how polyglutamylation generated by the two predominant neuronal polyglutamylases, TTLL1 and TTLL7, specifically modulates the activities of three major microtubule interactors: the microtubule-associated protein Tau, the microtubule-severing enzyme katanin and the molecular motor kinesin-1. We demonstrate that the unique modification patterns generated by TTLL1 and TTLL7 differentially impact those three effector proteins, thus allowing for their selective regulation. Given that our experiments were performed with brain tubulin from mouse models in which physiological levels and patterns of polyglutamylation were altered by the genetic knockout of the main modifying enzymes, our quantitative measurements provide direct mechanistic insight into how polyglutamylation could selectively control microtubule interactions in neurons.
ER  -

GENOVA, Mariya; Lenka GRYCOVA; Verena PUTTRICH; Maria M MAGIERA; Zdenek LANSKY; Carsten JANKE a Marcus BRAUN. Tubulin polyglutamylation differentially regulates microtubule-interacting proteins. \textit{EMBO Journal}. Hoboken (USA): WILEY-BLACKWELL, 2023, roč.~42, č.~5, s.~1-17. ISSN~0261-4189. Dostupné z: https://doi.org/10.15252/embj.2022112101.

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