| First Author | Saito Y | Year | 2003 |
| Journal | Exp Cell Res | Volume | 286 |
| Issue | 2 | Pages | 233-40 |
| PubMed ID | 12749852 | Mgi Jnum | J:172890 |
| Mgi Id | MGI:5009181 | Doi | 10.1016/s0014-4827(03)00054-5 |
| Citation | Saito Y, et al. (2003) Identification of alpha-tubulin as an hsp105alpha-binding protein by the yeast two-hybrid system. Exp Cell Res 286(2):233-40 |
| abstractText | Hsp105alpha is a mammalian stress protein that belongs to the HSP105/110 family. Hsp105alpha prevents stress-induced apoptosis in neuronal cells and binds to Hsp70/Hsc70 and suppresses the Hsp70 chaperone activity in vitro. In this study, to further elucidate the function of Hsp105alpha, we searched for Hsp105alpha-binding proteins by screening a mouse FM3A cell cDNA library with full-length Hsp105alpha using the yeast two-hybrid system and obtained alpha-tubulin as an Hsp105alpha-binding protein. Hsp105alpha bound directly to alpha-tubulin both in vitro and in vivo. Indirect immunofluorescence analysis with anti-Hsp105 and anti-alpha-tubulin antibodies indicated that Hsp105alpha was colocalized with microtubules. Furthermore, the disorganization of microtubules induced by heat shock was prevented in Hsp105alpha-overexpressing COS-7 cells. These findings suggested that Hsp105alpha associates with alpha-tubulin and microtubules in cells and plays a role in protection of microtubules under conditions of stress. |
