Abstract
Dynein is a large, multisubunit molecular motor that translocates cargoes toward the minus end of microtubules. It contains 2 heavy chains (DHC), several intermediate chains (DIC) and light intermediate chains (DLIC) and a number of light chains (DLC). Specific assembly of the various subunits has to be precise to ensure functioning of Dynein. The intermediate chain (DIC) of cytoplasmic dynein binds to the highly conserved 8-kDa light chain (DLC-8) through a highly conserved 10 aa stretch (reads SYSKETQTPL). A yeast 2-hybrid screen using DLC-8 as bait showed that a wide variety of additional partners exist and that DLC-8 binding proteins contain the consensus sequence (K/R)XTQT. The motif interacts with the common target-accepting grooves of DCL-8 dimer.The motif forms a beta-strand structure in the DLC-8-target peptide complex. Because it binds to a large number of functionally unrelated proteins DCL-8 is believed to act as a multifunctional regulatory protein.
Selected references
This ELM has been assigned the following Gene Ontology (GO) terms for biological process, cellular component and molecular function.
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Biological Process |
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microtubule-based movement
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Cellular Component |
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cytosol |
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cytoplasmic dynein complex |
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dynein complex |
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Molecular Function |
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protein binding |
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dynein light chain binding |
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