Article
|
Open Access
Featured
-
-
Letter |
Directionality of dynein is controlled by the angle and length of its stalk
The motility of dynein towards the minus end of the microtubule is controlled by the length and angle of the coiled-coil stalk that connects the motor to the microtubule.
- Sinan Can
- , Samuel Lacey
- & Ahmet Yildiz
-
Letter |
Structure of human cytoplasmic dynein-2 primed for its power stroke
The X-ray crystal structure of the human cytoplasmic dynein-2 motor bound to the ATP-hydrolysis transition state analogue ADP.vanadate is described.
- Helgo Schmidt
- , Ruta Zalyte
- & Andrew P. Carter
-
Letter |
Large-scale vortex lattice emerging from collectively moving microtubules
Emergent collective behaviour is observed in dynein-driven microtubules and modelled by taking into account only local interactions and the reptation-like motion of individual microtubules.
- Yutaka Sumino
- , Ken H. Nagai
- & Kazuhiro Oiwa
-
Letter |
Small-molecule inhibitors of the AAA+ ATPase motor cytoplasmic dynein
A family of small molecules called ‘ciliobrevins’ are described that can rapidly and reversibly modulate the AAA+ ATPase motor dynein, which transports cargo molecules along microtubule tracks.
- Ari J. Firestone
- , Joshua S. Weinger
- & James K. Chen
-
Article |
The 2.8 Å crystal structure of the dynein motor domain
The crystal structure of the entire motor domain of cytoplasmic dynein at the highest resolution so far is presented, giving insights into the communication between the different subdomains of the motor.
- Takahide Kon
- , Takuji Oyama
- & Genji Kurisu
-
News & Views |
A staggering giant
The protein dynein 'walks' along filaments to transport various cargoes within the cell. Two studies reveal that, unlike other motor proteins, dynein's steps are not strictly coordinated.
- Wilhelm J. Walter
- & Stefan Diez
Axonemal structures reveal mechanoregulatory and disease mechanisms