scholarly journals Engagement of the Small GTPase Rab31 Protein and Its Effector, Early Endosome Antigen 1, Is Important for Trafficking of the Ligand-bound Epidermal Growth Factor Receptor from the Early to the Late Endosome

2014 ◽  
Vol 289 (18) ◽  
pp. 12375-12389 ◽  
Author(s):  
Christelle En Lin Chua ◽  
Bor Luen Tang
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Growth Factor Receptor ◽  
Early Endosome ◽  
Small Gtpase ◽  
Late Endosome ◽  
Epidermal Growth

scholarly journals MICAL-like1 mediates epidermal growth factor receptor endocytosis

2011 ◽  
Vol 22 (18) ◽  
pp. 3431-3441 ◽  
Author(s):  
Nancy Abou-Zeid ◽  
Rudy Pandjaitan ◽  
Lucie Sengmanivong ◽  
Violaine David ◽  
Gwenaelle Le Pavec ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Fluorescent Protein ◽  
Coiled Coil ◽  
Growth Factor Receptor ◽  
Time Lapse ◽  
Small Gtpase ◽  
Rab Protein ◽  
Epidermal Growth

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

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