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

Stefano Pernigo, Magda Chegkazi, Yan Y. Yip, Conor Treacy, Giulia Glorani, Kjetil Hansen, Argyris Politis, Mark P. Dodding, View ORCID ProfileRoberto A. Steiner
doi: https://doi.org/10.1101/322057
Stefano Pernigo
Randall Centre of Cell and Molecular Biophysics, Faculty of Life Sciences and Medicine, King’s College London, London SE1 1UL, UK
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Magda Chegkazi
Randall Centre of Cell and Molecular Biophysics, Faculty of Life Sciences and Medicine, King’s College London, London SE1 1UL, UK
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Yan Y. Yip
Randall Centre of Cell and Molecular Biophysics, Faculty of Life Sciences and Medicine, King’s College London, London SE1 1UL, UK
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Conor Treacy
Randall Centre of Cell and Molecular Biophysics, Faculty of Life Sciences and Medicine, King’s College London, London SE1 1UL, UK
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Giulia Glorani
Randall Centre of Cell and Molecular Biophysics, Faculty of Life Sciences and Medicine, King’s College London, London SE1 1UL, UK
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Kjetil Hansen
Department of Chemistry, King’s College London Britannia House 7 Trinity Street, London, SE1 1DB (UK)
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Argyris Politis
Department of Chemistry, King’s College London Britannia House 7 Trinity Street, London, SE1 1DB (UK)
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Mark P. Dodding
Randall Centre of Cell and Molecular Biophysics, Faculty of Life Sciences and Medicine, King’s College London, London SE1 1UL, UK
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  • For correspondence: roberto.steiner@kcl.ac.uk mark.dodding@bristol.ac.uk
Roberto A. Steiner
Randall Centre of Cell and Molecular Biophysics, Faculty of Life Sciences and Medicine, King’s College London, London SE1 1UL, UK
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  • ORCID record for Roberto A. Steiner
  • For correspondence: roberto.steiner@kcl.ac.uk mark.dodding@bristol.ac.uk
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Abstract

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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Posted May 14, 2018.
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Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors
Stefano Pernigo, Magda Chegkazi, Yan Y. Yip, Conor Treacy, Giulia Glorani, Kjetil Hansen, Argyris Politis, Mark P. Dodding, Roberto A. Steiner
bioRxiv 322057; doi: https://doi.org/10.1101/322057
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Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors
Stefano Pernigo, Magda Chegkazi, Yan Y. Yip, Conor Treacy, Giulia Glorani, Kjetil Hansen, Argyris Politis, Mark P. Dodding, Roberto A. Steiner
bioRxiv 322057; doi: https://doi.org/10.1101/322057

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