EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules.
Curr Biol
; 32(18): 3898-3910.e14, 2022 09 26.
Article
de En
| MEDLINE
| ID: mdl-35963242
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 É-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.
Mots clés
Texte intégral:
1
Collection:
01-internacional
Base de données:
MEDLINE
Sujet principal:
Tubuline
/
Microtubules
Limites:
Humans
Langue:
En
Journal:
Curr Biol
Sujet du journal:
BIOLOGIA
Année:
2022
Type de document:
Article
Pays d'affiliation:
États-Unis d'Amérique