N-terminome analyses underscore the prevalence of SPPL3-mediated intramembrane proteolysis among Golgi-resident enzymes and its role in Golgi enzyme secretion

• Published in: Cellular and molecular life sciences : CMLS Vol. 79; no. 3; p. 185
• Main Authors: Hobohm, Laura, Koudelka, Tomas, Bahr, Fenja H., Truberg, Jule, Kapell, Sebastian, Schacht, Sarah-Sophie, Meisinger, Daniel, Mengel, Marion, Jochimsen, Alexander, Hofmann, Anna, Heintz, Lukas, Tholey, Andreas, Voss, Matthias
• Format: Journal Article
• Language: English
• Published: Cham Springer International Publishing 01.03.2022; Springer Nature B.V
• Subjects: Aspartic Acid Endopeptidases - deficiency; Aspartic Acid Endopeptidases - genetics; Aspartic Acid Endopeptidases - metabolism; Biochemistry; Biomedical and Life Sciences; Biomedicine; Catalytic Domain - genetics; Cell Biology; Cell culture; Cell lines; Cleavage; Enzymes; Extracellular glycosylation; FUT7; GALNT2; Gene Editing; Glycan; Glycosylation; Glycosyltransferase; Golgi apparatus; Golgi Apparatus - metabolism; HEK293 Cells; HeLa Cells; Humans; Intramembrane proteolysis; Life Sciences; Lipids; Membrane proteins; Membranes; Mucin; Mutagenesis, Site-Directed; N-Acetylgalactosaminyltransferases - genetics; N-Acetylgalactosaminyltransferases - metabolism; Original; Original Article; Physiology; Polypeptide N-acetylgalactosaminyltransferase; Protease; Proteinase; Proteins; Proteolysis; Proteome - analysis; Proteomes; Proteomics - methods; RNA, Guide, CRISPR-Cas Systems; Serum glycosyltransferases; SPPL3; Substrate Specificity; Substrates; Transmembrane domains; Serum glycosyltransferases; FUT7; GALNT2; SPPL3; Intramembrane proteolysis; Extracellular glycosylation

Golgi membrane proteins such as glycosyltransferases and other glycan-modifying enzymes are key to glycosylation of proteins and lipids. Secretion of soluble Golgi enzymes that are released from their membrane anchor by endoprotease activity is a wide-spread yet largely unexplored phenomenon. The in...