Melo-Hanchuk TD, Kobarg J. Polyglutamylase activity of tubulin tyrosine ligase-like 4 is negatively regulated by the never in mitosis gene A family kinase never in mitosis gene A -related kinase 5. World J Biol Chem 2021; 12(3): 38-51 [PMID: 34084286 DOI: 10.4331/wjbc.v12.i3.38]
Corresponding Author of This Article
Jörg Kobarg, PhD, Full Professor, Faculty of Pharmaceutical Sciences, University of Campinas, 200 Cândido Portinari, Campinas 13083-862, Brazil. jorgkoba@unicamp.br
Research Domain of This Article
Biochemistry & Molecular Biology
Article-Type of This Article
Basic Study
Open-Access Policy of This Article
This article is an open-access article which was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution Non Commercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/licenses/by-nc/4.0/
World J Biol Chem. May 27, 2021; 12(3): 38-51 Published online May 27, 2021. doi: 10.4331/wjbc.v12.i3.38
Polyglutamylase activity of tubulin tyrosine ligase-like 4 is negatively regulated by the never in mitosis gene A family kinase never in mitosis gene A -related kinase 5
Talita Diniz Melo-Hanchuk, Jörg Kobarg
Talita Diniz Melo-Hanchuk, Faculty of Pharmaceutical Sciences, Unicamp, Campinas 13083-862, Brazil
Jörg Kobarg, Faculty of Pharmaceutical Sciences, University of Campinas, Campinas 13083-862, Brazil
Author contributions: Melo-Hanchuk TD performed the experiments and interpreted them together with Kobarg J; both authors wrote the manuscript; Kobarg J supervised the project.
Supported byFundação de Amparo à Pesquisa do Estado São Paulo (FAPESP; São Paulo, Brazil) through Grant Temático, No. 2017/03489-1.
Institutional review board statement: The study was reviewed and approved by the Institutional review board of UNICAMP.
Conflict-of-interest statement: Both authors declare they have no conflict of interest.
Data sharing statement: Data will be made available upon reasonable request.
Open-Access: This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: http://creativecommons.org/Licenses/by-nc/4.0/
Corresponding author: Jörg Kobarg, PhD, Full Professor, Faculty of Pharmaceutical Sciences, University of Campinas, 200 Cândido Portinari, Campinas 13083-862, Brazil. jorgkoba@unicamp.br
Received: October 25, 2020 Peer-review started: October 25, 2020 First decision: December 24, 2020 Revised: January 6, 2021 Accepted: February 25, 2021 Article in press: February 25, 2021 Published online: May 27, 2021 Processing time: 212 Days and 13.7 Hours
Core Tip
Core Tip: Tubulins are modified extensively by post-translational processes such as polyglutamylation. Considering the diversity of microtubule polyglutamylation and the existence of many non-tubulin substrates, it is important to understand how the effector enzymes, the tubulin ligase-like (TTLL) proteins, are regulated. TTLL4 interacts with never in mitosis gene A (NIMA)-related kinase 5, a member of the mitotic NIMA-related kinases. We demonstrate that NIMA-related kinase 5 is a potential regulator of polyglutamylation through the control of TTLL4 activity. Here we show, for the time, the regulation of TTLL4 activity through phosphorylation, and demonstrate the potential control of polyglutamylation through NEK family members in human cells.
