Journal
MOLECULAR BIOLOGY OF THE CELL
Volume 23, Issue 21, Pages 4226-4241Publisher
AMER SOC CELL BIOLOGY
DOI: 10.1091/mbc.E12-03-0210
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Funding
- Dutch Ministry of Economic Affairs (BSIK)
- Netherlands Organization for Scientific Research (NWO-ALW VICI)
- Netherlands Organization for Health Research and Development (ZonMw-TOP) grants
- Foundation for Fundamental Research on Matter program grant
- Human Frontier Science Program grant
- National Institutes of Health [RO1 NS48501]
- University of Missouri Research Board
- Netherlands Organization for Scientific Research (NWO-ALW)
- Netherlands Organization for Scientific Research (NWO-ECHO)
- Netherlands Organization for Health Research and Development (ZonMw-VIDI)
- Netherlands Organization for Health Research and Development (ZonMw-TOP)
- European Science Foundation
- Human Frontier Science Program Career Development Award (HFSP-CDA)
- European Community [241548]
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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.
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