{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pernigo S"],"funding":["Biotechnology and Biological Sciences Research Council"],"pagination":["e38362"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6214655"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["7"],"pubmed_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 (KLC<sup>TPR</sup>). 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 KLC1<sup>TPR</sup> 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 i"],"journal":["eLife"],"pubmed_title":["Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors."],"pmcid":["PMC6214655"],"funding_grant_id":["BB/S000917/1","BB/S000828/1","BB/L006774/1"],"pubmed_authors":["Bui S","Dodding MP","Politis A","Steiner RA","Hansen K","Yip YY","Chegkazi MS","Treacy C","Glorani G","Pernigo S"],"additional_accession":[]},"is_claimable":false,"name":"Structural basis for isoform-specific kinesin-1 recognition of Y-acidic cargo adaptors.","description":"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 (KLC<sup>TPR</sup>). 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 KLC1<sup>TPR</sup> 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 i","dates":{"release":"2018-01-01T00:00:00Z","publication":"2018 Oct","modification":"2026-05-03T02:57:26.188Z","creation":"2019-03-27T00:06:32Z"},"accession":"S-EPMC6214655","cross_references":{"pubmed":["30320553"],"doi":["10.7554/eLife.38362"]}}