Vasohibins encode tubulin detyrosinating activity

Author:

Nieuwenhuis Joppe1ORCID,Adamopoulos Athanassios1,Bleijerveld Onno B.1ORCID,Mazouzi Abdelghani1ORCID,Stickel Elmer1ORCID,Celie Patrick1,Altelaar Maarten12ORCID,Knipscheer Puck34ORCID,Perrakis Anastassis1ORCID,Blomen Vincent A.1ORCID,Brummelkamp Thijn R.145ORCID

Affiliation:

1. Division of Biochemistry, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, Netherlands.

2. Biomolecular Mass Spectrometry and Proteomics, Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, 3584 CH Utrecht, Netherlands.

3. Hubrecht Institute–KNAW, University Medical Center Utrecht, 3584 CT Utrecht, Netherlands.

4. CGC.nl, Plesmanlaan 121, 1066 CX Amsterdam, Netherlands.

5. CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, 1090 Vienna, Austria.

Abstract

Tubulin carboxypeptidase identity revealed Enzymes of the α-tubulin detyrosination/tyrosination cycle create landmarks on microtubules that are essential for their multiple cellular functions and are altered in disease. Tubulin carboxypeptidases (TCPs) responsible for detyrosination have remained elusive for 40 years (see the Perspective by Akhmanova and Maiato). Aillaud et al. identified vasohibins as enzymes that perform the TCP function and found that their small interacting partner SBVP was essential for their activity. Vasohibin/SVBP complexes were involved in neuron polarization and brain cortex development. The authors also developed an inhibitor targeting this family of enzymes. Using a completely different strategy, Nieuwenhuis et al. also showed that vasohibins can remove the C-terminal tyrosine of α-tubulin. Science , this issue p. 1448 , p. 1453 ; see also p. 1381

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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