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1. ALS2CL, the novel protein highly homologous to the carboxy-terminal half of ALS2, binds to Rab5 and modulates endosome dynamics

Author

Asako Otomo, Yoshiko Yanagisawa, Kyoko Suzuki-Utsunomiya, Shinji Hadano, Joh-E Ikeda, Ryota Kunita, Hikaru Mizumura, and Junko Showguchi-Miyata

Subjects
Endosome, Molecular Sequence Data, Biophysics, Endosomes, Biology, environment and public health, Biochemistry, Guanine-nucleotide exchange factor, HeLa, Mice, Rab5, Structural Biology, Endosome dynamics, Genetics, Homologous chromosome, Animals, Guanine Nucleotide Exchange Factors, Humans, Tissue Distribution, Small GTPase, Amino Acid Sequence, Molecular Biology, ALS2 carboxy-terminal like, Adaptor Proteins, Signal Transducing, rab5 GTP-Binding Proteins, Amyotrophic Lateral Sclerosis, fungi, Dynamics (mechanics), Amyotrophic lateral sclerosis 2, Colocalization, Cell Biology, biology.organism_classification, Phenotype, Molecular biology, Protein Structure, Tertiary, Alternative Splicing, enzymes and coenzymes (carbohydrates), Guanine nucleotide exchange factor, biological phenomena, cell phenomena, and immunity, Carrier Proteins, Sequence Alignment, HeLa Cells, Protein Binding, Subcellular Fractions
Abstract

ALS2, the causative gene product for juvenile recessive amyotrophic lateral sclerosis (ALS2), is a guanine-nucleotide exchange factor for the small GTPase Rab5. Here, we report a novel ALS2 homologous gene, ALS2 C-terminal like (ALS2CL), which encodes a 108-kD ALS2CL protein. ALS2CL exhibited a specific but a relatively weak Rab5-GEF activity with accompanying rather strong Rab5-binding properties. In HeLa cells, co-expression of ALS2CL and Rab5A resulted in a unique tubulation phenotype of endosome compartments with significant colocalization of ALS2CL and Rab5A. These results suggest that ALS2CL is a novel factor modulating the Rab5-mediated endosome dynamics in the cells.

Published
2004
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2. Defective relocalization of ALS2/alsin missense mutants to Rac1-induced macropinosomes accounts for loss of their cellular function and leads to disturbed amphisome formation

Author

Ryota Kunita, Shinji Hadano, Asako Otomo, Joh-E Ikeda, and Kyoko Suzuki-Utsunomiya

Subjects
rac1 GTP-Binding Protein, Autophagosome, ALS2, Endosome, Mutant, Mutation, Missense, Biophysics, RAC1, Endosomes, Biology, Biochemistry, Phosphatidylinositol Phosphates, Amphisome, Structural Biology, Phagosomes, Genetics, Guanine Nucleotide Exchange Factors, Humans, Macropinosome, Molecular Biology, rab5 GTP-Binding Proteins, Activator (genetics), Pinocytosis, Cell Biology, Protein Structure, Tertiary, Cell biology, Protein Transport, Mutant Proteins, Guanine nucleotide exchange factor, Rac1, HeLa Cells, Protein Binding
Abstract

Loss of ALS2/alsin function accounts for several recessive motor neuron diseases. ALS2 is a Rab5 activator and its endosomal localization is regulated by Rac1 via macropinocytosis. Here, we show that the pathogenic missense ALS2 mutants fail to be localized to Rac1-induced macropinosomes as well as endosomes, which leads to loss of the ALS2 function as a Rab5 activator on endosomes. Further, these mutants lose the competence to enhance the formation of amphisomes, the hybrid-organelle formed upon fusion between autophagosomes and endosomes. Thus, Rac1-induced relocalization of ALS2 might be crucial to exert the ALS2 function associated with the autophagy-endolysosomal degradative pathway.Structured summaryRac1physically interactswithALS2 by pull down(View interaction)Rab5Aphysically interactswithALS2 by pull down(View Interaction1,2)ALS2 and EEA1colocalize by fluorescence microscopy(View Interaction1,2,3)ALS2physically interactswithALS2 by anti tag coimmunoprecipitation(View interaction)

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