Detyrosination is a form ofposttranslational modification that occurs on alpha-tubulin.[1] It consists of the removal of theC-terminaltyrosine to expose aglutamate at the newly formed C-terminus. Tubulin polymers, calledmicrotubules, that contain detyrosinated alpha-tubulin are usually referred to asGlu-microtubules while unmodified polymers are calledTyr-microtubules.
The detyrosynating activity was first identified in the late 1970s.[2] It is a slow acting enzyme that uses polymeric tubulin as a substrate. As a result, only stabilized microtubules accumulate this particular modification. Tubulin detyrosination is reversed by thetubulin-tyrosine ligase,[3] which acts only on alpha-tubulin monomer. Since the majority of microtubules are very dynamic, they do not contain much detyrosinated tubulin.
Vasohibins/SVBP are tubulin carboxypeptidases (TCPs) that regulate neuron differentiation.
Aillaud C, Bosc C, Peris L, Bosson A, Heemeryck P, Van Dijk J, Le Friec J, Boulan B, Vossier F, Sanman LE, Syed S, Amara N, Couté Y, Lafanechère L, Denarier E, Delphin C, Pelletier L, Humbert S, Bogyo M, Andrieux A, Rogowski K, Moutin MJ.
Science. 2017 Dec 15;358(6369):1448-1453. doi: 10.1126/science.aao4165. Epub 2017 Nov 16.
PMID: 29146868