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Kinesin-1 captures RNA cargo in its adaptable coils

The prototypic and ubiquitous microtubule motor, kinesin-1, uses a variety of adaptor proteins to facilitate the selective transport of diverse cargo within the cell. These cargo adaptors bind to the motor complex through interactions with the kinesin light or heavy chains (KLCs or KHCs). In this is...

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Detalles Bibliográficos
Autores principales: Cross, Jessica A., Woolfson, Derek. N., Dodding, Mark P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Cold Spring Harbor Laboratory Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8247605/
https://www.ncbi.nlm.nih.gov/pubmed/34210804
http://dx.doi.org/10.1101/gad.348691.121
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author Cross, Jessica A.
Woolfson, Derek. N.
Dodding, Mark P.
author_facet Cross, Jessica A.
Woolfson, Derek. N.
Dodding, Mark P.
author_sort Cross, Jessica A.
collection PubMed
description The prototypic and ubiquitous microtubule motor, kinesin-1, uses a variety of adaptor proteins to facilitate the selective transport of diverse cargo within the cell. These cargo adaptors bind to the motor complex through interactions with the kinesin light or heavy chains (KLCs or KHCs). In this issue of Genes & Development, Dimitrova-Paternoga et al. (pp. 976–991) present the first structural characterization of a KHC–cargo adaptor interface. They describe an antiparallel heterotrimeric coiled-coil complex between the carboxy tail of KHC and Tm1-I/C (aTm1), the atypical tropomyosin that is important for oskar mRNA transport in Drosophila oocytes. This interaction enhances direct binding between KHC and RNA. Their findings demonstrate the structural plasticity of the KHC tail as a platform for protein–protein interactions and reveal how a cargo adaptor protein can modify a motor–RNA interface to promote transport.
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spelling pubmed-82476052021-07-20 Kinesin-1 captures RNA cargo in its adaptable coils Cross, Jessica A. Woolfson, Derek. N. Dodding, Mark P. Genes Dev Outlook The prototypic and ubiquitous microtubule motor, kinesin-1, uses a variety of adaptor proteins to facilitate the selective transport of diverse cargo within the cell. These cargo adaptors bind to the motor complex through interactions with the kinesin light or heavy chains (KLCs or KHCs). In this issue of Genes & Development, Dimitrova-Paternoga et al. (pp. 976–991) present the first structural characterization of a KHC–cargo adaptor interface. They describe an antiparallel heterotrimeric coiled-coil complex between the carboxy tail of KHC and Tm1-I/C (aTm1), the atypical tropomyosin that is important for oskar mRNA transport in Drosophila oocytes. This interaction enhances direct binding between KHC and RNA. Their findings demonstrate the structural plasticity of the KHC tail as a platform for protein–protein interactions and reveal how a cargo adaptor protein can modify a motor–RNA interface to promote transport. Cold Spring Harbor Laboratory Press 2021-07-01 /pmc/articles/PMC8247605/ /pubmed/34210804 http://dx.doi.org/10.1101/gad.348691.121 Text en © 2021 Cross et al.; Published by Cold Spring Harbor Laboratory Press https://creativecommons.org/licenses/by/4.0/This article, published in Genes & Development, is available under a Creative Commons License (Attribution 4.0 International), as described at http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Outlook
Cross, Jessica A.
Woolfson, Derek. N.
Dodding, Mark P.
Kinesin-1 captures RNA cargo in its adaptable coils
title Kinesin-1 captures RNA cargo in its adaptable coils
title_full Kinesin-1 captures RNA cargo in its adaptable coils
title_fullStr Kinesin-1 captures RNA cargo in its adaptable coils
title_full_unstemmed Kinesin-1 captures RNA cargo in its adaptable coils
title_short Kinesin-1 captures RNA cargo in its adaptable coils
title_sort kinesin-1 captures rna cargo in its adaptable coils
topic Outlook
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8247605/
https://www.ncbi.nlm.nih.gov/pubmed/34210804
http://dx.doi.org/10.1101/gad.348691.121
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