title: The neural adhesion molecule L1 is phosphorylated on tyrosine and serine residues.
abstract: The neural cell adhesion molecule L1 is highly homologous in its extracellular domain between species and completely identical in its cytoplasmic domain. We report here that tyrosine residues of L1 are phosphorylated in addition to serine residues, as determined by monoclonal phosphotyrosine antibodies and phosphoamino acid analysis. This result supports the suggestion that the cytoplasmic domain of L1 might be involved in signal transduction.
authors.affiliation: Biochemical Department of the Institute of Animal Physiology and Anatomy, University of Bonn, Germany.
authors.forename: P C
authors.initials: PC
authors.lastname: Heiland
authors.forename: B
authors.initials: B
authors.lastname: Hertlein
authors.forename: O
authors.initials: O
authors.lastname: Traub
authors.forename: L S
authors.initials: LS
authors.lastname: Griffith
authors.forename: B
authors.initials: B
authors.lastname: Schmitz
mesh_terms: D000818:Animals; D001345:Autoradiography; D015816:Cell Adhesion Molecules, Neuronal / Q000378:metabolism*; D002478:Cells, Cultured; D002531:Cerebellum / Q000378:metabolism*; D051379:Mice; D008815:Mice, Inbred Strains; D012694:Serine / Q000378:metabolism*; D014443:Tyrosine / Q000378:metabolism*
chemical_list: D015816:Cell Adhesion Molecules, Neuronal; D014443:Tyrosine; D012694:Serine