MICAL-like1 mediates epidermal growth factor receptor endocytosis

• DOI: 10.1091/mbc.e11-01-0030
• Publication Date: 2011-07-28T03:45:20Z
• Authors: Nancy Abou-Zeid; Rudy Pandjaitan; Lucie Sengmanivong; Violaine David; Gwenaelle Le Pavec; Jean Salamero; Ahmed Zahraoui
• Keywords: Rab; Transport protein; Small GTPase

Small GTPase Rabs are required for membrane protein sorting/delivery to precise domains. Rab13 regulates epithelial tight junction assembly and polarized transport. Here we report that Molecule Interacting with CasL (MICAL)-like1 (MICAL-L1) interacts GTP-Rab13 shares a similar domain organization MICAL. MICAL-L1 has calponin homology (CH), LIM, proline rich coiled-coil It is associated late endosomes. Time-lapse video microscopy shows green fluorescent protein-Rab7 mcherry-MICAL-L1 present within vesicles move rapidly in the cytoplasm. Depletion of by short hairpin RNA does not alter distribution endosome/lysosome-associated but affects trafficking epidermal growth factor receptor (EGFR). Overexpression leads accumulation EGFR endosomal compartment. In contrast, knocking down results internalized spread throughout cytoplasm promotes its degradation. Our data suggest N-terminal CH associates C-terminal binding (RBD) MICAL-L1. The RBD disrupts CH/RBD interaction, may induce conformational change MICAL-L1, promoting activation. provide novel insights into MICAL-L1/Rab complex can regulate at endocytic pathways.