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ALS2CL, the novel protein highly homologous to the carboxy‐terminal half of ALS2, binds to Rab5 and modulates endosome dynamics
Author(s) -
Hadano Shinji,
Otomo Asako,
Suzuki-Utsunomiya Kyoko,
Kunita Ryota,
Yanagisawa Yoshiko,
Showguchi-Miyata Junko,
Mizumura Hikaru,
Ikeda Joh-E
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.07.092
Subject(s) - endosome , guanine nucleotide exchange factor , colocalization , microbiology and biotechnology , gene product , biology , gtpase , gene , chemistry , gene expression , biochemistry , intracellular
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.