Masking of Transmembrane-Based Retention Signals Controls ER Export of γ-Secretase

• Published in: Traffic (Copenhagen, Denmark) Vol. 11; no. 2; pp. 250 - 258
• Main Authors: Fassler, Matthias, Zocher, Michael, Klare, Sebastian, de la Fuente, Alerie Guzman, Scheuermann, Johanna, Capell, Anja, Haass, Christian, Valkova, Christina, Veerappan, Anbazhagan, Schneider, Dirk, Kaether, Christoph
• Format: Journal Article
• Language: English
• Published: Oxford, UK Oxford, UK : Blackwell Publishing Ltd 01.02.2010; Blackwell Publishing Ltd
• Subjects: Alzheimer disease; Alzheimer's disease; Amyloid Precursor Protein Secretases - chemistry; Amyloid Precursor Protein Secretases - genetics; Amyloid Precursor Protein Secretases - metabolism; Animals; Cell Line; Endoplasmic Reticulum - metabolism; ER retention/retrieval; Humans; Immunoblotting; Mice; Microscopy, Fluorescence; presenilin; Presenilins - chemistry; Presenilins - genetics; Protein Binding; Protein Sorting Signals; Protein Structure, Tertiary; Protein Transport; transmembrane domain; γ-secretase

γ-Secretase is critically involved in the Notch pathway and in Alzheimer's disease. The four subunits of γ-secretase assemble in the endoplasmic reticulum (ER) and unassembled subunits are retained/retrieved to the ER by specific signals. We here describe a novel ER-retention/retrieval signal i...