Article
- The EMBO Journal (2003) 22, 6004 - 6015
- doi:10.1093/emboj/cdg592
Subject Categories:
Bicaudal D induces selective dynein-mediated microtubule minus end-directed transport
Casper C. Hoogenraad1, Phebe Wulf1, Natalia Schiefermeier2, Tatiana Stepanova3, Niels Galjart3, J. Victor Small2, Frank Grosveld3, Chris I. de Zeeuw1 and Anna Akhmanova3
- MGC Departments of Neuroscience, Erasmus University, PO Box 1738, 3000 DR Rotterdam, The Netherlands
- Institute of Molecular Biology, Austrian Academy of Sciences, Billrothsthstrasse 11, Salzburg 5020, Austria
- MGC Departments of Cell Biology and Genetics, Erasmus University, PO Box 1738, 3000 DR Rotterdam, The Netherlands
Correspondence to:
Anna Akhmanova, E-mail: anna.akhmanova@chello.nl
Received 15 May 2003; Accepted 2 October 2003; Revised 10 September 2003
Abstract
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.
Keywords:
- cytoplasmic dynein,
- dynactin,
- kinesin,
- mitochondria,
- peroxisomes
