title: Nuclear translocation of intracellular domain of Protogenin by proteolytic cleavage.
abstract: Protogenin (PRTG) is a transmembrane protein of immunoglobulin superfamily, which has multiple roles in embryogenesis as a receptor or an adhesion molecule. In this study, we present sequential proteolytic cleavage of PRTG. The cleavage first occurs at the extracellular domain, then at the interface of the transmembrane and the intracellular domain by γ-secretase, which results in the release of the intracellular domain of PRTG (PRTG-ICD). PRTG-ICD contains putative nuclear localization signal (NLS) at its N-terminal, and translocates to the nucleus in cultured cells and in the neuroepithelial cells of chick embryos. We propose that the PRTG-ICD is cleaved by γ-secretase and translocates to the nucleus, which is potentially implicated in signaling for neural differentiation and in cell adhesion mediated by PRTG.
authors.affiliation: Department of Molecular Neurobiology, Graduate School of Life Sciences, Tohoku University, Aoba-ku, Sendai, Japan. yuji@idac.tohoku.ac.jp
authors.forename: Yuji
authors.initials: Y
authors.lastname: Watanabe
authors.forename: Harukazu
authors.initials: H
authors.lastname: Nakamura
mesh_terms: D053829:Amyloid Precursor Protein Secretases / Q000378:metabolism; D000818:Animals; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism*; D002642:Chick Embryo; D006801:Humans; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D021381:Protein Transport / Q000502:physiology
chemical_list: D008565:Membrane Proteins; D053829:Amyloid Precursor Protein Secretases