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Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors

By Stefano Pernigo, Magda Chegkazi, Yan Y. Yip, Conor Treacy, Giulia Glorani, Kjetil Hansen, Argyris Politis, Mark P Dodding, Roberto A. Steiner

Posted 14 May 2018
bioRxiv DOI: 10.1101/322057 (published DOI: 10.7554/elife.38362)

The light chains (KLCs) of the heterotetrameric microtubule motor kinesin-1, that bind to cargo adaptor proteins and regulate its activity, have a capacity to recognize short peptides via their tetratricopeptide repeat domains (KLCTPR). Here, using X-ray crystallography, we show how kinesin-1 recognizes a novel class of adaptor motifs that we call Y-acidic (tyrosine flanked by acidic residues), in a KLC-isoform specific manner. Binding specificities of Y-acidic motifs (present in JIP1 and in TorsinA) to KLC1TPR are distinct from those utilized for the recognition of W-acidic motifs found in adaptors that are KLC-isoform non-selective. However, a partial overlap on their receptor binding sites implies that adaptors relying on Y-acidic and W-acidic motifs must act independently. We propose a model to explain why these two classes of motifs that bind to the concave surface of KLCTPR with similar low micromolar affinity can exhibit different capacities to promote kinesin-1 activity.

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