論文 - 詳細
| RRC ID | 86915 |
|---|---|
| 著者 | Kawaguchi K, Hama Y, Yoshikawa H, Nishino K, Morimoto K, Nakamura T, Koizumi M, Sakamaki Y, Abe K, Kakuta S, Ichimura K, Ikeda F, Kosako H, Fujita N. |
| タイトル | Linear ubiquitination triggers Amph-mediated T-tubule biogenesis. |
| ジャーナル | Sci Adv |
| Abstract |
Transverse tubules (T-tubules) are invaginations of the muscle plasma membrane that facilitate rapid transmission of action potentials, ensuring synchronized muscle contraction. Despite their essential role in muscle physiology, the mechanisms underlying T-tubule formation remain elusive. Here, we identify LUBEL/RNF31, a ubiquitin E3 ligase responsible for linear (M1-linked) ubiquitination, as a key regulator of T-tubule biogenesis in Drosophila. Loss of LUBEL leads to Amphiphysin (Amph)-positive membrane sheets instead of tubular networks. The ubiquitin ligase activity of LUBEL and direct interaction with Amph, a BAR domain protein involved in membrane tubulation, are crucial for proper T-tubule morphology. LUBEL and M1-linked ubiquitin chains assemble into puncta on membranes through multivalent interactions, facilitating Amph-mediated tubulation. Notably, the Amph-LUBEL/RNF31 interaction is evolutionarily conserved across species, underscoring a fundamental role for linear ubiquitination in membrane remodeling. Our findings uncover an unexpected function of linear ubiquitination in membrane deformation driven by BAR proteins. |
| 巻・号 | 12(2) |
| ページ | eady4934 |
| 公開日 | 2026-1-9 |
| DOI | 10.1126/sciadv.ady4934 |
| PMID | 41499502 |
| PMC | PMC12778051 |
| MeSH | Animals Cell Membrane / metabolism Drosophila / metabolism Drosophila Proteins* / genetics Drosophila Proteins* / metabolism Drosophila melanogaster / metabolism Nerve Tissue Proteins Protein Binding Ubiquitin-Protein Ligases* / genetics Ubiquitin-Protein Ligases* / metabolism Ubiquitination* |
| IF | 13.117 |
| オルトメトリクス指標 |
オルトメトリクス指標項目
|
| 最多言及媒体 | News |
| 各媒体での言及数の合計 | 5 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 17.0 |
| リソース情報 | |
| ショウジョウバエ | 11321R-2 |