Kinesin-1 captures RNA cargo in its adaptable coils

  1. Mark P. Dodding1
  1. 1School of Biochemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TD, United Kingdom;
  2. 2School of Chemistry, Faculty of Life Sciences, University of Bristol, Bristol BS8 1TS, United Kingdom;
  3. 3Bristol BioDesign Institute, University of Bristol, Bristol BS8 1TQ, United Kingdom
  1. Corresponding author: mark.dodding{at}bristol.ac.uk

Abstract

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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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/.

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