Tubulin Polyglutamylation by TTLL1 and TTLL7 Regulate Glutamate Concentration in the Mice Brain

Yashuang Ping; Kenji Ohata; Kenji Kikushima; Takumi Sakamoto; Ariful Islam; Lili Xu; Hengsen Zhang; Bin Chen; Jing Yan; Fumihiro Eto; Chiho Nakane; Keizo Takao; Tsuyoshi Miyakawa; Katsuya Kabashima; Miho Watanabe; Tomoaki Kahyo; Ikuko Yao; Atsuo Fukuda; Koji Ikegami; Yoshiyuki Konishi; Mitsutoshi Setou

doi:10.3390/biom13050784

Tubulin Polyglutamylation by TTLL1 and TTLL7 Regulate Glutamate Concentration in the Mice Brain

Yashuang Ping
, Kenji Ohata
, Kenji Kikushima
, Takumi Sakamoto
, Ariful Islam
, Lili Xu
, Hengsen Zhang
, Bin Chen
, Jing Yan
, Fumihiro Eto
, Chiho Nakane
, Keizo Takao
, Tsuyoshi Miyakawa
, Katsuya Kabashima
, Miho Watanabe
, Tomoaki Kahyo
, Ikuko Yao
, Atsuo Fukuda
, Koji Ikegami
, Yoshiyuki Konishi

Mitsutoshi Setou

Research output: Contribution to journal › Article › peer-review

4 Citations (Scopus)

Abstract

As an important neurotransmitter, glutamate acts in over 90% of excitatory synapses in the human brain. Its metabolic pathway is complicated, and the glutamate pool in neurons has not been fully elucidated. Tubulin polyglutamylation in the brain is mainly mediated by two tubulin tyrosine ligase-like (TTLL) proteins, TTLL1 and TTLL7, which have been indicated to be important for neuronal polarity. In this study, we constructed pure lines of Ttll1 and Ttll7 knockout mice. Ttll knockout mice showed several abnormal behaviors. Matrix-assisted laser desorption/ionization (MALDI) Imaging mass spectrometry (IMS) analyses of these brains showed increases in glutamate, suggesting that tubulin polyglutamylation by these TTLLs acts as a pool of glutamate in neurons and modulates some other amino acids related to glutamate.

Original language	English
Article number	784
Journal	Biomolecules
Volume	13
Issue number	5
DOIs	https://doi.org/10.3390/biom13050784
Publication status	Published - 05-2023
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry
Molecular Biology

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10.3390/biom13050784

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Ping, Y., Ohata, K., Kikushima, K., Sakamoto, T., Islam, A., Xu, L., Zhang, H., Chen, B., Yan, J., Eto, F., Nakane, C., Takao, K., Miyakawa, T., Kabashima, K., Watanabe, M., Kahyo, T., Yao, I., Fukuda, A., Ikegami, K., ... Setou, M. (2023). Tubulin Polyglutamylation by TTLL1 and TTLL7 Regulate Glutamate Concentration in the Mice Brain. Biomolecules, 13(5), Article 784. https://doi.org/10.3390/biom13050784

@article{ba24b0515fc44c4db91989b5545645a3,

title = "Tubulin Polyglutamylation by TTLL1 and TTLL7 Regulate Glutamate Concentration in the Mice Brain",

abstract = "As an important neurotransmitter, glutamate acts in over 90\% of excitatory synapses in the human brain. Its metabolic pathway is complicated, and the glutamate pool in neurons has not been fully elucidated. Tubulin polyglutamylation in the brain is mainly mediated by two tubulin tyrosine ligase-like (TTLL) proteins, TTLL1 and TTLL7, which have been indicated to be important for neuronal polarity. In this study, we constructed pure lines of Ttll1 and Ttll7 knockout mice. Ttll knockout mice showed several abnormal behaviors. Matrix-assisted laser desorption/ionization (MALDI) Imaging mass spectrometry (IMS) analyses of these brains showed increases in glutamate, suggesting that tubulin polyglutamylation by these TTLLs acts as a pool of glutamate in neurons and modulates some other amino acids related to glutamate.",

author = "Yashuang Ping and Kenji Ohata and Kenji Kikushima and Takumi Sakamoto and Ariful Islam and Lili Xu and Hengsen Zhang and Bin Chen and Jing Yan and Fumihiro Eto and Chiho Nakane and Keizo Takao and Tsuyoshi Miyakawa and Katsuya Kabashima and Miho Watanabe and Tomoaki Kahyo and Ikuko Yao and Atsuo Fukuda and Koji Ikegami and Yoshiyuki Konishi and Mitsutoshi Setou",

note = "Publisher Copyright: {\textcopyright} 2023 by the authors.",

year = "2023",

month = may,

doi = "10.3390/biom13050784",

language = "English",

volume = "13",

journal = "Biomolecules",

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Ping, Y, Ohata, K, Kikushima, K, Sakamoto, T, Islam, A, Xu, L, Zhang, H, Chen, B, Yan, J, Eto, F, Nakane, C, Takao, K, Miyakawa, T, Kabashima, K, Watanabe, M, Kahyo, T, Yao, I, Fukuda, A, Ikegami, K, Konishi, Y & Setou, M 2023, 'Tubulin Polyglutamylation by TTLL1 and TTLL7 Regulate Glutamate Concentration in the Mice Brain', Biomolecules, vol. 13, no. 5, 784. https://doi.org/10.3390/biom13050784

TY - JOUR

T1 - Tubulin Polyglutamylation by TTLL1 and TTLL7 Regulate Glutamate Concentration in the Mice Brain

AU - Ping, Yashuang

AU - Ohata, Kenji

AU - Kikushima, Kenji

AU - Sakamoto, Takumi

AU - Islam, Ariful

AU - Xu, Lili

AU - Zhang, Hengsen

AU - Chen, Bin

AU - Yan, Jing

AU - Eto, Fumihiro

AU - Nakane, Chiho

AU - Takao, Keizo

AU - Miyakawa, Tsuyoshi

AU - Kabashima, Katsuya

AU - Watanabe, Miho

AU - Kahyo, Tomoaki

AU - Yao, Ikuko

AU - Fukuda, Atsuo

AU - Ikegami, Koji

AU - Konishi, Yoshiyuki

AU - Setou, Mitsutoshi

PY - 2023/5

Y1 - 2023/5

N2 - As an important neurotransmitter, glutamate acts in over 90% of excitatory synapses in the human brain. Its metabolic pathway is complicated, and the glutamate pool in neurons has not been fully elucidated. Tubulin polyglutamylation in the brain is mainly mediated by two tubulin tyrosine ligase-like (TTLL) proteins, TTLL1 and TTLL7, which have been indicated to be important for neuronal polarity. In this study, we constructed pure lines of Ttll1 and Ttll7 knockout mice. Ttll knockout mice showed several abnormal behaviors. Matrix-assisted laser desorption/ionization (MALDI) Imaging mass spectrometry (IMS) analyses of these brains showed increases in glutamate, suggesting that tubulin polyglutamylation by these TTLLs acts as a pool of glutamate in neurons and modulates some other amino acids related to glutamate.

AB - As an important neurotransmitter, glutamate acts in over 90% of excitatory synapses in the human brain. Its metabolic pathway is complicated, and the glutamate pool in neurons has not been fully elucidated. Tubulin polyglutamylation in the brain is mainly mediated by two tubulin tyrosine ligase-like (TTLL) proteins, TTLL1 and TTLL7, which have been indicated to be important for neuronal polarity. In this study, we constructed pure lines of Ttll1 and Ttll7 knockout mice. Ttll knockout mice showed several abnormal behaviors. Matrix-assisted laser desorption/ionization (MALDI) Imaging mass spectrometry (IMS) analyses of these brains showed increases in glutamate, suggesting that tubulin polyglutamylation by these TTLLs acts as a pool of glutamate in neurons and modulates some other amino acids related to glutamate.

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DO - 10.3390/biom13050784

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AN - SCOPUS:85160376377

SN - 2218-273X

VL - 13

JO - Biomolecules

JF - Biomolecules

IS - 5

M1 - 784

ER -

Tubulin Polyglutamylation by TTLL1 and TTLL7 Regulate Glutamate Concentration in the Mice Brain

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