Cargando…
Coupling of ATPase activity, microtubule binding, and mechanics in the dynein motor domain
The movement of a molecular motor protein along a cytoskeletal track requires communication between enzymatic, polymer‐binding, and mechanical elements. Such communication is particularly complex and not well understood in the dynein motor, an ATPase that is comprised of a ring of six AAA domains, a...
Autores principales: | Niekamp, Stefan, Coudray, Nicolas, Zhang, Nan, Vale, Ronald D, Bhabha, Gira |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6600642/ https://www.ncbi.nlm.nih.gov/pubmed/31268607 http://dx.doi.org/10.15252/embj.2018101414 |
Ejemplares similares
-
Lis1 Acts as a “Clutch” between the ATPase and Microtubule-Binding Domains of the Dynein Motor
por: Huang, Julie, et al.
Publicado: (2012) -
Helix sliding in the stalk coiled coil of dynein couples ATPase and microtubule binding
por: Kon, Takahide, et al.
Publicado: (2009) -
Nanometer-accuracy distance measurements between fluorophores at the single-molecule level
por: Niekamp, Stefan, et al.
Publicado: (2019) -
Cytoplasmic dynein crosslinks and slides anti-parallel microtubules using its two motor domains
por: Tanenbaum, Marvin E, et al.
Publicado: (2013) -
Review: Structure and mechanism of the dynein motor ATPase
por: Schmidt, Helgo, et al.
Publicado: (2016)