title: Signal transduction: stuck with FYVE domains.
abstract: The FYVE domain is a protein motif that allows the interaction of cytosolic proteins with membranes containing the lipid phosphatidylinositol 3-phosphate. Structural information about FYVE domains has come from two crystal structures and NMR analysis. Corvera discusses how these structures differ and what they tell us about how proteins with FYVE domains interact with biological membranes. The Perspective also addresses how proteins with FYVE domains and protein internalization are involved in signal transduction.
authors.affiliation: Program in Molecular Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA. silvia.corvera@umassmed.edu
authors.forename: S
authors.initials: S
authors.lastname: Corvera
mesh_terms: D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D003545:Cysteine; D011992:Endosomes / Q000502:physiology*; D006801:Humans; D018129:Phosphatidylinositol Phosphates / Q000502:physiology*; D011485:Protein Binding; D011506:Proteins / Q000502:physiology*; D015398:Signal Transduction
chemical_list: D018129:Phosphatidylinositol Phosphates; D011506:Proteins; C055525:phosphatidylinositol 3-phosphate; D003545:Cysteine