EML2-S Constitutes a New Class of Proteins That Recognizes and Regulates the Dynamics of Tyrosinated Microtubules

Takashi Hotta,Thomas S. McAlear,Yang Yue,Takumi Higaki,Sarah E. Haynes,Alexey I. Nesvizhskii,David Sept,Kristen J. Verhey,Susanne Bechstedt,Ryoma Ohi

Current Biology（2022）SCI 1区

Univ Michigan | McGill Univ | Kumamoto Univ

Cited 8|Views35

Abstract

Tubulin post-translational modifications (PTMs) alter microtubule properties by affecting the binding of microtubule-associated proteins (MAPs). Microtubule detyrosination, which occurs by proteolytic removal of the C-terminal tyrosine from ɑ-tubulin, generates the oldest known tubulin PTM, but we lack comprehensive knowledge of MAPs that are regulated by this PTM. We developed a screening pipeline to identify proteins that discriminate between Y- and ΔY-microtubules and found that echinoderm microtubule-associated protein-like 2 (EML2) preferentially interacts with Y-microtubules. This activity depends on a Y-microtubule interaction motif built from WD40 repeats. We show that EML2 tracks the tips of shortening microtubules, a behavior not previously seen among human MAPs in vivo, and influences dynamics to increase microtubule stability. Our screening pipeline is readily adapted to identify proteins that specifically recognize a wide range of microtubule PTMs.

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Key words

microtubule,tyrosination,post-translational modification,tubulin code,echinoderm microtubule-associated protein,WD repeat

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