Bicaudal D induces selective dynein-mediated microtubule minus end-directed transport.
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Bicaudal D is an evolutionarily conserved protein, which is involved in dynein-mediated motility both in Drosophila and in mammals. Here we report that the N-terminal portion of human Bicaudal D2 (BICD2) is capable of inducing microtubule minus end-directed movement independently of the molecular context. This characteristic offers a new tool to exploit the relocalization of different cellular components by using appropriate targeting motifs. Here, we use the BICD2 N-terminal domain as a chimera with mitochondria and peroxisome-anchoring sequences to demonstrate the rapid dynein-mediated transport of selected organelles. Surprisingly, unlike other cytoplasmic dynein-mediated processes, this transport shows very low sensitivity to overexpression of the dynactin subunit dynamitin. The dynein-recruiting activity of the BICD2 N-terminal domain is reduced within the full-length molecule, indicating that the C-terminal part of the protein might regulate the interaction between BICD2 and the motor complex. Our findings provide a novel model system for dissection of the molecular mechanism of dynein motility.
- Research Support, Non-U.S. Gov't
- Recombinant Fusion Proteins/genetics/metabolism
- Genes, Reporter
- Membrane Proteins/genetics/metabolism
- Drosophila Proteins/genetics/*metabolism
- Dynein ATPase/*metabolism
- Microtubule-Associated Proteins/metabolism
- Microtubule-Organizing Center/metabolism