PIGN prevents protein aggregation in the endoplasmic reticulum independently of its function in the GPI synthesis

• Published in: Journal of cell science Vol. 130; no. 3; pp. 602 - 613
• Main Authors: Ihara, Shinji, Nakayama, Sohei, Murakami, Yoshiko, Suzuki, Emiko, Asakawa, Masayo, Kinoshita, Taroh, Sawa, Hitoshi
• Format: Journal Article
• Language: English
• Published: England The Company of Biologists Ltd 01.02.2017
• Subjects: Agglomeration; Anchors; Animals; Biosynthesis; Caenorhabditis elegans - cytology; Caenorhabditis elegans - metabolism; Caenorhabditis elegans - ultrastructure; Caenorhabditis elegans Proteins - metabolism; Conserved Sequence; CRISPR; Endoplasmic reticulum; Endoplasmic Reticulum - metabolism; Endoplasmic Reticulum - ultrastructure; Evolution, Molecular; Glycosylphosphatidylinositol; Glycosylphosphatidylinositols - metabolism; HEK293 Cells; Humans; Intracellular Membranes - metabolism; Intracellular Space - metabolism; Mammalian cells; Mutation; Mutation - genetics; Nematodes; Phosphotransferases - chemistry; Phosphotransferases - metabolism; Protein Aggregates; Protein interaction; Proteins; Quality control; Sequence Homology, Amino Acid; GPI; MCAHS1 patients; Protein aggregation; PIGN; Endoplasmic reticulum

Quality control of proteins in the endoplasmic reticulum (ER) is essential for ensuring the integrity of secretory proteins before their release into the extracellular space. Secretory proteins that fail to pass quality control form aggregates. Here we show the PIGN-1/PIGN is required for quality co...