Structural biology of cytoplasmic and axonemal dyneins

Dyneins are microtubule-based, ATP-driven motor proteins with six tandemly linked AAA+ domains, a long N-terminal tail and a coiled-coil stalk. Cytoplasmic dyneins function as individual homodimers and are responsible for minus-end-oriented transport along microtubules. Axonemal dyneins of flagella/...

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Bibliographic Details
Published in:Journal of structural biology 2012-08, Vol.179 (2), p.229-234
Main Author: Ishikawa, Takashi
Format: Article
Language:English
Subjects:
AAA protein
Axonemal Dyneins - chemistry
Axonemal Dyneins - metabolism
Cilia
Crystallography, X-Ray
Cytoplasm - metabolism
Dynein
Dyneins - chemistry
Dyneins - metabolism
Flagella
Microscopy, Electron
Motor protein
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Summary:Dyneins are microtubule-based, ATP-driven motor proteins with six tandemly linked AAA+ domains, a long N-terminal tail and a coiled-coil stalk. Cytoplasmic dyneins function as individual homodimers and are responsible for minus-end-oriented transport along microtubules. Axonemal dyneins of flagella/cilia are anchored in arrays to peripheral microtubule doublets by their N-terminal tails, and generate sliding motions of adjacent microtubule doublets toward the plus end. The coiled-coil stalk is responsible for communication between the AAA+ domains and the microtubule binding domain. A number of isoforms of axonemal dyneins are integrated to generate bending motion. In this article I will review recent structural studies and address the question as to how dyneins generate force and cause bending in flagella/cilia.
ISSN:1047-8477
1095-8657
DOI:10.1016/j.jsb.2012.05.016