Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules

Lis1 is a key cofactor for the assembly of active cytoplasmic dynein complexes that transport cargo along microtubules. Lis1 binds to the AAA+ ring and stalk of dynein and slows dynein motility, but the underlying mechanism has remained unclear. Using single-molecule imaging and optical trapping ass...

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Veröffentlicht in:	Nature chemical biology 2024-04, Vol.20 (4), p.521-529
Hauptverfasser:	Kusakci, Emre, Htet, Zaw Min, Zhao, Yuanchang, Gillies, John P., Reck-Peterson, Samara L., Yildiz, Ahmet
Format:	Artikel
Sprache:	eng
Schlagworte:	631/136/334/2243 631/57/2265 631/80 631/92/173 Asymmetry Binding sites Biochemical Engineering Biochemistry Bioorganic Chemistry Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Cytoplasmic Dyneins - metabolism Dynein Dyneins - chemistry Microtubule-Associated Proteins - metabolism Microtubules Microtubules - metabolism Motility Mutagenesis Optical trapping Saccharomyces cerevisiae - metabolism Sliding Tethering Yeasts
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