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Mol Biol Cell. 2012 Nov;23(21):4226-41. doi: 10.1091/mbc.E12-03-0210. Epub 2012 Sep 5.

BICD2, dynactin, and LIS1 cooperate in regulating dynein recruitment to cellular structures.

Author information

1
Department of Cell Biology, Erasmus Medical Centre, 3000 CA Rotterdam, Netherlands Department of Neuroscience, Erasmus Medical Centre, 3000 CA Rotterdam, The Netherlands.

Abstract

Cytoplasmic dynein is the major microtubule minus-end-directed cellular motor. Most dynein activities require dynactin, but the mechanisms regulating cargo-dependent dynein-dynactin interaction are poorly understood. In this study, we focus on dynein-dynactin recruitment to cargo by the conserved motor adaptor Bicaudal D2 (BICD2). We show that dynein and dynactin depend on each other for BICD2-mediated targeting to cargo and that BICD2 N-terminus (BICD2-N) strongly promotes stable interaction between dynein and dynactin both in vitro and in vivo. Direct visualization of dynein in live cells indicates that by itself the triple BICD2-N-dynein-dynactin complex is unable to interact with either cargo or microtubules. However, tethering of BICD2-N to different membranes promotes their microtubule minus-end-directed motility. We further show that LIS1 is required for dynein-mediated transport induced by membrane tethering of BICD2-N and that LIS1 contributes to dynein accumulation at microtubule plus ends and BICD2-positive cellular structures. Our results demonstrate that dynein recruitment to cargo requires concerted action of multiple dynein cofactors.

PMID:
22956769
PMCID:
PMC3484101
DOI:
10.1091/mbc.E12-03-0210
[Indexed for MEDLINE]
Free PMC Article

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