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Bicaudal D induces selective dynein‐mediated microtubule minus end‐directed transport
Author(s) -
Hoogenraad Casper C.,
Wulf Phebe,
Schiefermeier Natalia,
Stepanova Tatiana,
Galjart Niels,
Small J. Victor,
Grosveld Frank,
de Zeeuw Chris I.,
Akhmanova Anna
Publication year - 2003
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/cdg592
Subject(s) - dynein , dynactin , biology , microbiology and biotechnology , microtubule , motor protein , kinesin , microtubule associated protein , molecular motor , protein subunit , genetics , gene
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.