InterPro domain: IPR037177

Dynein is a multisubunit microtubule-dependent motor enzyme that acts as the force generating protein of eukaryotic cilia and flagella. The cytoplasmic isoform of dynein acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules.

Dynein is composed of a number of ATP-binding large subunits (see IPR004273 ), intermediate size subunits and small subunits. Among the small subunits, there is a family of highly conserved proteins which make up this family [ 1 , 2 , 3 ]. Proteins in this family act as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function and may play a role in changing or maintaining the spatial distribution of cytoskeletal structures. In yeast, it was identified as a component of the nuclear pore complex where it may contribute to the stable association of the Nup82 subcomplex with the nuclear pore complex [ 4 ].

Both type 1 (DLC1) and 2 (DLC2) dynein light chains have a similar two-layer alpha-beta core structure consisting of beta-alpha(2)-beta-X-beta(2) [ 5 , 6 ].

1. The M(r) = 8,000 and 11,000 outer arm dynein light chains from Chlamydomonas flagella have cytoplasmic homologues. J. Biol. Chem. 270, 11445-52
2. Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster. Mol. Cell. Biol. 16, 1966-77
3. Structural basis for assembly and function of the Nup82 complex in the nuclear pore scaffold. J Cell Biol 208, 283-97
4. Molecular basis for the functional interaction of dynein light chain with the nuclear-pore complex. Nat Cell Biol 9, 788-96
5. Structure of the PIN/LC8 dimer with a bound peptide. Nat. Struct. Biol. 6, 735-40
6. Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands. Biochem. J. 377, 597-605