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@article{1120463,
author = {Liu, Yang and Salter, Hannah K and Holding, Andrew N and Johnson, Christopher M and Stephens, Elaine and Lukavsky, Peter and Walshaw, John and Bullock, Simon L},
article_location = {COLD SPRING HARBOR},
article_number = {11},
doi = {http://dx.doi.org/10.1101/gad.212381.112},
keywords = {Bicaudal-D; coiled coil; dynein; cargo binding; crystal structure; Drosophila},
language = {eng},
issn = {0890-9369},
journal = {GENES & DEVELOPMENT},
title = {Bicaudal-D uses a parallel, homodimeric coiled coil with heterotypic registry to coordinate recruitment of cargos to dynein},
url = {http://genesdev.cshlp.org/content/27/11/1233.abstract},
volume = {27},
year = {2013}
}
TY - JOUR
ID - 1120463
AU - Liu, Yang - Salter, Hannah K - Holding, Andrew N - Johnson, Christopher M - Stephens, Elaine - Lukavsky, Peter - Walshaw, John - Bullock, Simon L
PY - 2013
TI - Bicaudal-D uses a parallel, homodimeric coiled coil with heterotypic registry to coordinate recruitment of cargos to dynein
JF - GENES & DEVELOPMENT
VL - 27
IS - 11
SP - 1233-1246
EP - 1233-1246
PB - COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT
SN - 08909369
KW - Bicaudal-D
KW - coiled coil
KW - dynein
KW - cargo binding
KW - crystal structure
KW - Drosophila
UR - http://genesdev.cshlp.org/content/27/11/1233.abstract
L2 - http://genesdev.cshlp.org/content/27/11/1233.abstract
N2 - Cytoplasmic dynein is the major minus end-directed microtubule motor in eukaryotes. However, there is little structural insight into how different cargos are recognized and linked to the motor complex. Here we describe the 2.2 angstrom resolution crystal structure of a cargo-binding region of the dynein adaptor Bicaudal-D (BicD), which reveals a parallel coiled-coil homodimer. We identify a shared binding site for two cargo-associated proteins-Rab6 and the RNA-binding protein Egalitarian (Egl)-within a region of the BicD structure with classical, homotypic core packing. Structure-based mutagenesis in Drosophila provides evidence that occupancy of this site drives association of BicD with dynein, thereby coupling motor recruitment to cargo availability. The structure also contains a region in which, remarkably, the same residues in the polypeptide sequence have different heptad registry in each chain. In vitro and in vivo analysis of a classical Drosophila dominant mutation reveals that this heterotypic region regulates the recruitment of dynein to BicD. Our results support a model in which the heterotypic segment is part of a molecular switch that promotes release of BicD autoinhibition following cargo binding to the neighboring, homotypic coiled-coil region. Overall, our data reveal a pivotal role of a highly asymmetric coiled-coil domain in coordinating the assembly of cargo-motor complexes.
ER -
LIU, Yang, Hannah K SALTER, Andrew N HOLDING, Christopher M JOHNSON, Elaine STEPHENS, Peter LUKAVSKY, John WALSHAW and Simon L BULLOCK. Bicaudal-D uses a parallel, homodimeric coiled coil with heterotypic registry to coordinate recruitment of cargos to dynein. \textit{GENES \&{} DEVELOPMENT}. COLD SPRING HARBOR: COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT, 2013, vol.~27, No~11, p.~1233-1246. ISSN~0890-9369. Available from: https://dx.doi.org/10.1101/gad.212381.112.
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