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.
Highlights
Dimitrova-Paternoga et al (2021) explore the role of the atypical tropomyosin, Tm1-I/C, that is important for oskar mRNA localization to the posterior pole of the Drosophila oocyte
The KHC–aTm1 complex is shown to bind RNA with higher affinity than KHC only, suggesting a new mechanism by which kinesin–cargo (RNA) transport can be modulated through stabilization by a KHC cargo adaptor
This is likely due to the positively charged binding surface formed in the trimeric KHC–aTm1 complex and possible stabilization of an extended helical region of the KHC tail
Summary
Dimitrova-Paternoga et al (2021) explore the role of the atypical tropomyosin, Tm1-I/C (aTm1), that is important for oskar mRNA localization to the posterior pole of the Drosophila oocyte. The KHC–aTm1 complex is shown to bind RNA with higher affinity than KHC only, suggesting a new mechanism by which kinesin–cargo (RNA) transport can be modulated through stabilization by a KHC cargo adaptor.
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