Structural insights into microtubule doublet interactions in axonemes.
Coordinated sliding of microtubule doublets, driven by dynein motors, produces periodic beating of eukaryotic cilia and flagella. Recent structural studies of the axoneme, which forms the core of cilia and flagella, have used cryo-electron tomography to reveal new details of the interactions between some of the multitude of proteins that form the axoneme and regulate its movement. Connections between the several types of dyneins, in particular, suggest ways in which their action might be coordinated. Study of the molecular architecture of isolated doublets has provided a structural basis for understanding mechanical properties related to the bending of the axoneme, and has also offered insight into the potential role of doublets in the mechanism of dynein activity regulation.
Downing
Kenneth H
KH
Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, USA. khdowning@lbl.gov
Sui
Haixin
H
D000818:Animals; D002696:Chlamydomonas / Q000737:chemistry / Q000648:ultrastructure; D021621:Imaging, Three-Dimensional; D008870:Microtubules / Q000737:chemistry* / Q000648:ultrastructure; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000648:ultrastructure; D012617:Sea Urchins / Q000737:chemistry / Q000648:ultrastructure
D020409:Molecular Motor Proteins