A family of carboxypeptidases catalyzing α- and β-tubulin tail processing and deglutamylation

Author:

Nicot Simon1ORCID,Gillard Ghislain1ORCID,Impheng Hathaichanok2,Joachimiak Ewa3ORCID,Urbach Serge4ORCID,Mochizuki Kazufumi5ORCID,Wloga Dorota3,Juge François1ORCID,Rogowski Krzysztof1ORCID

Affiliation:

1. Tubulin Code team, Institute of Human Genetics, Université Montpellier, CNRS, Montpellier, France.

2. Department of Physiology, Faculty of Medical science, Naresuan University, Phitsanulok 65000, Thailand.

3. Laboratory of Cytoskeleton and Cilia Biology, Nencki Institute of Experimental Biology, Polish Academy of Sciences, 3 Pasteur Street, 02-093 Warsaw, Poland.

4. Functional Proteomics Platform (FPP), IGF, Université Montpellier, CNRS, INSERM, Montpellier, France.

5. Epigenetic Chromatin Regulation team, Institute of Human Genetics, Université Montpellier, CNRS, Montpellier, France.

Abstract

Tubulin posttranslational modifications represent an important mechanism involved in the regulation of microtubule functions. The most widespread among them are detyrosination, α∆2-tubulin, and polyglutamylation. Here, we describe a family of tubulin-modifying enzymes composed of two closely related proteins, KIAA0895L and KIAA0895, which have tubulin metallocarboxypeptidase activity and thus were termed TMCP1 and TMCP2, respectively. We show that TMCP1 (also known as MATCAP) acts as α-tubulin detyrosinase that also catalyzes α∆2-tubulin. In contrast, TMCP2 preferentially modifies βI-tubulin by removing three amino acids from its C terminus, generating previously unknown βI∆3 modification. We show that βI∆3-tubulin is mostly found on centrioles and mitotic spindles and in cilia. Moreover, we demonstrate that TMCPs also remove posttranslational polyglutamylation and thus act as tubulin deglutamylases. Together, our study describes the identification and comprehensive biochemical analysis of a previously unknown type of tubulin-modifying enzymes involved in the processing of α- and β-tubulin C-terminal tails and deglutamylation.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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