Dynein motors can move at a pretty fast pace of 2 microns in just 4 seconds.
And axonemal dyneins can move microtubules in a test tube at the remarkable rate of 14 μm/sec.
In comparison, the fastest kinesins can move their microtubules at about 2–3 μm/sec.
Dynein motors do walk and the dimeric microtubule-based motor proteins, kinesin-1 and cytoplasmic dynein can take over one hundred steps without detaching from the track.
Kinesins and dyneins are two families of molecular motors that walk along microtubules in opposite directions: dyneins walk toward the minus end of microtubules, whereas most kinesins walk toward the microtubule plus end.
The dynein is known to walk along the microtubules towards their minus-ends and because the microtubule minus-ends are embedded in the centrosome, minus-end directed motility of dynein results in a pulling force that brings the nucleus and centrosome towards each other.
Dynein is produced and found in many eukaryotes, including, fungi, worms, insects, and vertebrates, but analysis of Arabidopsis genome indicates that they are not found in plants.
These dyneins are the arms which project from the doublet axonemal microtubules of flagella and cilia.
The axonemal dyneins generate the sliding force between outer doublet microtubules that is converted by other axonemal structures into the bending of cilia and flagella.
The two types of dynein are cytoplasmic dyneins and axonemal dyneins, which are also called ciliary or flagellar dyneins.
Dyneins are a family of cytoskeletal motor proteins that move along microtubules in cells which convert the chemical energy stored in ATP to mechanical work.
Dynein transports various cellular cargos, provides forces and displacements important in mitosis, and drives the beat of eukaryotic cilia and flagella.
Phylogenetically, there are nine major classes of dynein heavy chain20.
The cytoplasmic dynein 1 heavy chain (encoded by DYNC1H1 in humans) is used for nearly all of the minus end-directed transport in the cytoplasm of most eukaryotic cells.
Cytoplasmic dynein-1 is responsible for the majority of transport toward microtubule minus ends in the cell interior.
Dynein-2, also known as intraflagellar transport dynein, moves cargoes along the axoneme of eukaryotic cilia and flagella.
Dynein is unique compared with kinesin and myosin because dynein molecules form large molecular complexes.
For example, one axonemal outer arm dynein molecule of C. reinhardtii is composed of three dynein heavy chains, two intermediate chains, and more than ten light chains.
Dyneins make up a family of AAA+ motors that move toward the minus end of microtubules.
Cytoplasmic dynein is responsible for transporting intracellular cargos in interphase cells and mediating spindle assembly and chromosome positioning during cell division.
The flagellar dyneins, also called axonemal dyneins, are the arms that project from the doublet axonemal microtubules of flagella and cilia.
The flagellar dyneins generate the sliding force between outer doublet microtubules that is converted by other axonemal structures into the bending of cilia and flagella.
Kinesin motor proteins are innately limited to unidirectional stepping, allowing for either anterograde or retrograde transport, with most kinesins performing anterograde transport.
Meanwhile, dynein is more likely to perform retrograde transport, although dynein motor proteins are capable of bidirectional stepping.