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/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.
Biomolecular Research Laboratory, Paul Scherrer Institute, Villigen PSI CH5232, Switzerland. takashi.ishikawa@psi.ch
Takashi
T
Ishikawa
D056444:Axonemal Dyneins / Q000737:chemistry* / Q000378:metabolism*; D018360:Crystallography, X-Ray; D003593:Cytoplasm / Q000378:metabolism*; D004398:Dyneins / Q000737:chemistry* / Q000378:metabolism*; D008854:Microscopy, Electron
D056444:Axonemal Dyneins; D004398:Dyneins