| First Author | Hadano S | Year | 2004 |
| Journal | FEBS Lett | Volume | 575 |
| Issue | 1-3 | Pages | 64-70 |
| PubMed ID | 15388334 | Mgi Jnum | J:92859 |
| Mgi Id | MGI:3054618 | Doi | 10.1016/j.febslet.2004.07.092 |
| Citation | Hadano S, et al. (2004) ALS2CL, the novel protein highly homologous to the carboxy-terminal half of ALS2, binds to Rab5 and modulates endosome dynamics. FEBS Lett 575(1-3):64-70 |
| abstractText | 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. |
