<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>22(18)</volume><submitter>Kizhatil K</submitter><pubmed_abstract>Doublecortin is a cytoplasmic protein mutated in the neuronal migration disorder X-linked lissencephaly. This study describes a novel activity of doublecortin in recognition of the FIGQY-phosphotyrosine motif present in the cytoplasmic domain of the L1 cell adhesion molecule neurofascin. Phospho-FIGQY-neurofascin (186 kDa) coimmunoprecipitated with doublecortin from detergent extracts of embryonic brain membranes, and this doublecortin-phospho-FIGQY neurofascin complex was disassociated by a synthetic phospho-FIGQY neurofascin peptide but not by a dephospho-FIGQY peptide. Doublecortin specifically recognized the phospho-FIGQY tyrosine in the context of a synthetic phospho-FIGQY neurofascin peptide and in phospho-FIGQY neurofascin isolated from cells treated with pervanadate. Mutations of d</pubmed_abstract><journal>The Journal of neuroscience : the official journal of the Society for Neuroscience</journal><pagination>7948-58</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6758080</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin.</pubmed_title><pmcid>PMC6758080</pmcid><pubmed_authors>Kizhatil K</pubmed_authors><pubmed_authors>Bennett V</pubmed_authors><pubmed_authors>Sen A</pubmed_authors><pubmed_authors>Wu YX</pubmed_authors></additional><is_claimable>false</is_claimable><name>A new activity of doublecortin in recognition of the phospho-FIGQY tyrosine in the cytoplasmic domain of neurofascin.</name><description>Doublecortin is a cytoplasmic protein mutated in the neuronal migration disorder X-linked lissencephaly. This study describes a novel activity of doublecortin in recognition of the FIGQY-phosphotyrosine motif present in the cytoplasmic domain of the L1 cell adhesion molecule neurofascin. Phospho-FIGQY-neurofascin (186 kDa) coimmunoprecipitated with doublecortin from detergent extracts of embryonic brain membranes, and this doublecortin-phospho-FIGQY neurofascin complex was disassociated by a synthetic phospho-FIGQY neurofascin peptide but not by a dephospho-FIGQY peptide. Doublecortin specifically recognized the phospho-FIGQY tyrosine in the context of a synthetic phospho-FIGQY neurofascin peptide and in phospho-FIGQY neurofascin isolated from cells treated with pervanadate. Mutations of d</description><dates><release>2002-01-01T00:00:00Z</release><publication>2002 Sep</publication><modification>2025-04-26T00:04:13.403Z</modification><creation>2019-10-11T07:10:24Z</creation></dates><accession>S-EPMC6758080</accession><cross_references><pubmed>12223548</pubmed><doi>10.1523/jneurosci.22-18-07948.2002</doi><doi>10.1523/JNEUROSCI.22-18-07948.2002</doi></cross_references></HashMap>