Journal article
Structural biology of cytoplasmic and axonemal dyneins.
- Ishikawa T Biomolecular Research Laboratory, Paul Scherrer Institute, Villigen PSI CH5232, Switzerland. takashi.ishikawa@psi.ch
- 2012-06-06
Published in:
- Journal of structural biology. - 2012
English
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.
- Language
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- English
- Open access status
- closed
- Identifiers
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- DOI 10.1016/j.jsb.2012.05.016
- PMID 22664481
- Persistent URL
- https://sonar.ch/global/documents/278452
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