Publication Name	World Journal of Biological Chemistry
Manuscript ID	60242
Country	Brazil

Category	Biochemistry & Molecular Biology
Manuscript Type	Basic Study
Article Title	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
Manuscript Source	Unsolicited Manuscript
All Author List	Talita Diniz Melo-Hanchuk and Jörg Kobarg
Funding Agency and Grant Number	Funding Agency Grant Number Fundação de Amparo à Pesquisa do Estado São Paulo (FAPESP; São Paulo, Brazil) through Grant Temático 2017/03489-1
Corresponding Author	Jörg Kobarg, PhD, Full Professor, Faculty of Pharmaceutical Sciences, University of Campinas, 200 Cândido Portinari, Campinas 13083-862, Brazil. jorgkoba@unicamp.br
Key Words	Kinase; Poly glutamylation; Never in mitosis gene A-related kinase 5; Tubulin tyrosine ligase like 4; Micotubles; Post translational regulation
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 tyrosine 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 NIMA-related kinase 5 as a potential regulator of polyglutamylation through TTLL4’s activity control. Here we provided the first relation of regulation of TTLL4 activity through phosphorylation, besides demonstrating the potential control of polyglutamylation through Nek family members in human cells.
Citation	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

Received	2020-10-25 17:28
Peer-Review Started	2020-10-25 17:29
To Make the First Decision
Return for Revision	2020-12-24 18:59
Revised	2021-01-06 19:41
Second Decision	2021-02-20 02:08
Accepted by Journal Editor-in-Chief
Accepted by Company Editor-in-Chief	2021-02-25 19:13
Articles in Press	2021-02-25 19:13
Publication Fee Transferred
Edit the Manuscript by Language Editor	2021-03-25 07:51
Typeset the Manuscript	2021-05-10 08:14

ISSN	1949-8454 (online)
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