Genome-wide CRISPR screen reveals CLPTM1L as a lipid scramblase required for efficient glycosylphosphatidylinositol biosynthesis

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 119; no. 14; pp. 1 - 11
• Main Authors: Wang, Yicheng, Menon, Anant K., Maki, Yuta, Liu, Yi-Shi, Iwasaki, Yugo, Fujita, Morihisa, Guerrero, Paula A., Silva, Daniel Varó’n, Seeberger, Peter H., Murakami, Yoshiko, Kinoshita, Taroh
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences 05.04.2022
• Subjects: Biological Sciences; Biosynthesis; Cell surface; Cleft lip/palate; Clustered Regularly Interspaced Short Palindromic Repeats; CRISPR; Cytosol; Endoplasmic reticulum; Endoplasmic Reticulum - metabolism; Genomes; Glycolipids; Glycosylphosphatidylinositol; Glycosylphosphatidylinositols - metabolism; Lipids; Lipogenesis; Membrane proteins; Membrane Proteins - genetics; Membrane Proteins - metabolism; Membranes; Phosphatidylinositol; Phospholipids; Proteins; Translocation; CLPTM1L; glycosylphosphatidylinositol; scramblase; endoplasmic reticulum; glycobiology

Glycosylphosphatidylinositols (GPIs) are complex glycolipids that act as membrane anchors of many eukaryotic cell surface proteins. Biosynthesis of GPIs is initiated at the cytosolic face of the endoplasmic reticulum (ER) by generation of N-acetylglucosaminyl-phosphatidylinositol (GlcNAc-PI). The se...