Cytoplasmic dynein carries cargo toward microtubule minus ends. Each motor is a ring of six AAA+ domains with a lever-like linker. A long stalk ends in a microtubule-binding foot. ATP binding closes the ring, primes the linker and releases the foot. Rebinding straightens the linker in the power stroke. Alone, human dynein-1 is mostly inactive. Dynactin and a cargo adaptor switch it on.
- Where
- Cytoplasm of most eukaryotic cells, on microtubules. It is absent from higher plants. Dynein-2 drives transport inside cilia.
- Power
- ATP hydrolysis, mainly at AAA1. AAA2 to AAA4 also bind nucleotide and tune the cycle.
6
AAA+ domains in the ring
327 pN
Stall force, yeast dynein
134.3 pN
Stall force, human dynein-dynactin-BICD2
20