Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 179, Issue 2, Pages 229-234Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2012.05.016
Keywords
Dynein; Flagella; Cilia; AAA protein; Motor protein
Funding
- Swiss National Science Foundation [NF31003A-125131/1]
- Swiss-Japan Cooperative Research Fund
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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. (C) 2012 Elsevier Inc. All rights reserved.
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