Abstract：
:The two related members of the vasohibin family, VASH1 and VASH2, encode human tubulin detyrosinases. Here we demonstrate that, in contrast to VASH1, which requires binding of small vasohibin binding protein (SVBP), VASH2 has autonomous tubulin detyrosinating activity. Moreover, we demonstrate that SVBP acts as a bona fide activator of both enzymes. Phylogenetic analysis of the vasohibin family revealed that regulatory diversification of VASH-mediated tubulin detyrosination coincided with early vertebrate evolution. Thus, as a model organism for functional analysis, we used Trypanosoma brucei (Tb), an evolutionarily early-branched eukaryote that possesses a single VASH and encodes a terminal tyrosine on both α- and β-tubulin tails, both subject to removal. Remarkably, although detyrosination levels are high in the flagellum, TbVASH knockout parasites did not present any noticeable flagellar abnormalities. In contrast, we observed reduced proliferation associated with profound morphological and mitotic defects, underscoring the importance of tubulin detyrosination in cell division.
journal_name
Cell Repjournal_title
Cell reportsauthors
van der Laan S,Lévêque MF,Marcellin G,Vezenkov L,Lannay Y,Dubra G,Bompard G,Ovejero S,Urbach S,Burgess A,Amblard M,Sterkers Y,Bastien P,Rogowski Kdoi
10.1016/j.celrep.2019.11.074subject
Has Abstractpub_date
2019-12-17 00:00:00pages
4159-4171.e6issue
12issn
2211-1247pii
S2211-1247(19)31565-7journal_volume
29pub_type
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