Differential roles of N- and C-terminal LIR motifs in the catalytic activity and membrane targeting of RavZ and ATG4B proteins

• DOI: 10.5483/bmbrep.2024-0084
• Publication Date: 2024-10-04T03:24:12Z
• Authors: Sang-Won Park; Ju-Hui Park; Haneul Choi; Pureum Jeon; Seung-Hwan Lee; Won-Dong Shin; Hun-Joo Kim; Jin-A Lee; Deok-Jin Jang
• Keywords: Motif (music)

Mammalian ATG8 proteins (mATG8s) are essential for selective autophagy because they recruit various with LC3- interacting region (LIR) motifs to autophagic membranes. The RavZ protein, secreted by Legionella pneumophila, and mammalian ATG4B possess functional LIR that participate in lipidated mATG8 deconjugation on comprises three at the N- Cterminal sides of its catalytic domain (CAD). This study demonstrated N-terminal side CAD involved membrane targeting substrate recognition, while motif C-terminal facilitate targeting. Our results also revealed human is pivotal delipidating LC3B-phosphatidylethanolamine (PE), but it plays a minor role pro-LC3B priming cytosol. Therefore, introducing does not affect LC3B-PE delipidation. clearly described position-dependent roles cellular contexts.