ALS2CL, the novel protein highly homologous to the carboxy‐terminal half of ALS2, binds to Rab5 and modulates endosome dynamics | Zendy

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

Premium

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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here

Accelerating Research