2022年9月26日
EML2-S constitutes a new class of proteins that recognizes and regulates the dynamics of tyrosinated microtubules.
Current biology : CB
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- 巻
- 32
- 号
- 18
- 開始ページ
- 3898
- 終了ページ
- 3910
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.cub.2022.07.027
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.
- リンク情報
- ID情報
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- DOI : 10.1016/j.cub.2022.07.027
- PubMed ID : 35963242
- PubMed Central 記事ID : PMC9530018