Bicaudal-D uses a parallel, homodimeric coiled coil with
heterotypic registry to coordinate recruitment of cargos to
dynein

J 2013

Bicaudal-D uses a parallel, homodimeric coiled coil with heterotypic registry to coordinate recruitment of cargos to dynein

LIU, Yang, Hannah K SALTER, Andrew N HOLDING, Christopher M JOHNSON, Elaine STEPHENS et. al.

Základní údaje

Originální název

Bicaudal-D uses a parallel, homodimeric coiled coil with heterotypic registry to coordinate recruitment of cargos to dynein

Autoři

LIU, Yang (826 Velká Británie a Severní Irsko), Hannah K SALTER (826 Velká Británie a Severní Irsko), Andrew N HOLDING (826 Velká Británie a Severní Irsko), Christopher M JOHNSON (826 Velká Británie a Severní Irsko), Elaine STEPHENS (826 Velká Británie a Severní Irsko), Peter LUKAVSKY (40 Rakousko, garant, domácí), John WALSHAW (826 Velká Británie a Severní Irsko) a Simon L BULLOCK (826 Velká Británie a Severní Irsko)

Vydání

GENES & DEVELOPMENT, COLD SPRING HARBOR, COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT, 2013, 0890-9369

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

Genetika a molekulární biologie

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 12.639

Kód RIV

RIV/00216224:14740/13:00069110

Organizační jednotka

Středoevropský technologický institut

DOI

http://dx.doi.org/10.1101/gad.212381.112

UT WoS

000320110000003

Klíčová slova anglicky

Bicaudal-D; coiled coil; dynein; cargo binding; crystal structure; Drosophila

Štítky

ok, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 4. 9. 2013 10:10, Olga Křížová

Anotace

V originále

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.

Návaznosti

ED1.1.00/02.0068, projekt VaV

Název: CEITEC - central european institute of technology

Citovat

LIU, Yang, Hannah K SALTER, Andrew N HOLDING, Christopher M JOHNSON, Elaine STEPHENS, Peter LUKAVSKY, John WALSHAW a Simon L BULLOCK. Bicaudal-D uses a parallel, homodimeric coiled coil with heterotypic registry to coordinate recruitment of cargos to dynein. GENES & DEVELOPMENT. COLD SPRING HARBOR: COLD SPRING HARBOR LAB PRESS, PUBLICATIONS DEPT, 2013, roč. 27, č. 11, s. 1233-1246. ISSN 0890-9369. Dostupné z: https://dx.doi.org/10.1101/gad.212381.112.

@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 a 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, roč.~27, č.~11, s.~1233-1246. ISSN~0890-9369. Dostupné z: https://dx.doi.org/10.1101/gad.212381.112.

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