InterPro domain: IPR013594

Dynein heavy chains interact with other heavy chains to form dimers, and with intermediate chain-light chain complexes to form a basal cargo binding unit [ 1 ]. The region featured in this family includes the sequences implicated in mediating these interactions [ 2 ]. It is thought to be flexible and not to adopt a rigid conformation [ 3 ].

Dyneins are described as motor proteins of eukaryotic cells, as they can convert energy derived from the hydrolysis of ATP to force and movement along cytoskeletal polymers, such as microtubules. Dyneins generally contain one to three heavy chains, which belong to the AAA+ superfamily of mechanochemical enzymes [ 3 ]. Each heavy chain consists of a flexible N-terminal tail known as the cargo-binding domain [ 4 ] and a motor domain which consists of an ATP-hydrolysing AAA+ ring, a flexible microtubule-binding stalk, a linker and a C-sequence [ 5 ]. The stalk has an ATP-sensitive microtubule-binding site (MTBD) at its tip [ 6 , 7 ], whereas the linker has been suggested to function as a mechanical element for generating dynein's power stroke [ 8 , 9 , 10 ].

The two categories of dyneins are the axonemal dyneins, which produce the bending motions that propagate along cilia and flagella, and the cytosolic dyneins, which drive a variety of fundamental cellular processes including nuclear migration, organisation of the mitotic spindle, chromosome separation during mitosis, and the positioning and function of many intracellular organelles. Cytoplasmic dyneins contain several accessory subunits ranging from light to intermediate chains.

1. AAA domains and organization of the dynein motor unit. J. Cell. Sci. 113 ( Pt 14), 2521-6
2. Interaction mapping of a dynein heavy chain. Identification of dimerization and intermediate-chain binding domains. J. Biol. Chem. 274, 15447-53
3. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9, 27-43
4. Recent progress in dynein structure and mechanism. Curr. Opin. Cell Biol. 17, 98-103
5. The 2.8 A crystal structure of the dynein motor domain. Nature 484, 345-50
6. An extended microtubule-binding structure within the dynein motor domain. Nature 390, 636-9
7. Identification of a microtubule-binding domain in a cytoplasmic dynein heavy chain. J Biol Chem 272, 19714-8
8. Dynein structure and power stroke. Nature 421, 715-8
9. AAA+ Ring and linker swing mechanism in the dynein motor. Cell 136, 485-95
10. ATP hydrolysis cycle-dependent tail motions in cytoplasmic dynein. Nat Struct Mol Biol 12, 513-9