Kinesin-1 captures RNA cargo in its adaptable coils

Jessica A A Cross, Dek N Woolfson, Mark P Dodding*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

1 Citation (Scopus)
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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 and Development, Dimitrova-Paternoga et al. present the first structural characterisation 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.
Original languageEnglish
Pages (from-to)937-939
Number of pages3
JournalGenes and Development
Issue number13-14
Publication statusPublished - 1 Jul 2021

Bibliographical note

Funding Information:
M.P.D. is a Lister Institute of Preventative Medicine Fellow, and work in his laboratory is supported by the Biotechnology and Biosciences Research Council (BB/S000917/1). J.A.C. is supported by the Engineering and Physical Sciences Research Council Bristol Centre for Doctoral Training in Chemical Synthesis.

Publisher Copyright:
© 2021 Cross et al.

Structured keywords

  • BCS and TECS CDTs


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