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-Structure paper
タイトル | CryoET reveals actin filaments within platelet microtubules. |
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ジャーナル・号・ページ | Nat Commun, Vol. 15, Issue 1, Page 5967, Year 2024 |
掲載日 | 2024年7月16日 |
著者 | Chisato Tsuji / Marston Bradshaw / Megan F Allen / Molly L Jackson / Judith Mantell / Ufuk Borucu / Alastair W Poole / Paul Verkade / Ingeborg Hers / Danielle M Paul / Mark P Dodding / |
PubMed 要旨 | Crosstalk between the actin and microtubule cytoskeletons is important for many cellular processes. Recent studies have shown that microtubules and F-actin can assemble to form a composite structure ...Crosstalk between the actin and microtubule cytoskeletons is important for many cellular processes. Recent studies have shown that microtubules and F-actin can assemble to form a composite structure where F-actin occupies the microtubule lumen. Whether these cytoskeletal hybrids exist in physiological settings and how they are formed is unclear. Here, we show that the short-crossover Class I actin filament previously identified inside microtubules in human HAP1 cells is cofilin-bound F-actin. Lumenal F-actin can be reconstituted in vitro, but cofilin is not essential. Moreover, actin filaments with both cofilin-bound and canonical morphologies reside within human platelet microtubules under physiological conditions. We propose that stress placed upon the microtubule network during motor-driven microtubule looping and sliding may facilitate the incorporation of actin into microtubules. |
リンク | Nat Commun / PubMed:39013865 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 20.0 Å |
構造データ | EMDB-50814: Real space helical reconstruction of cofilin actin in the microtubule lumen of human platelets EMDB-50845: Real space helical reconstruction of cofilin actin in the microtubule lumen of HAP1 cells |
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