Title

Bicd2, Dynactin, And Lis1 Cooperate In Regulating Dynein Recruitment To Cellular Structures

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. © 2012 Splinter et al.

Publication Date

11-1-2012

Publication Title

Molecular Biology of the Cell

Volume

23

Issue

21

Number of Pages

4226-4241

Document Type

Article

Personal Identifier

scopus

DOI Link

https://doi.org/10.1091/mbc.E12-03-0210

Socpus ID

84868250529 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/84868250529

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