Direct interaction of the beta-domain of VHL tumor suppressor protein with the regulatory domain of atypical PKC isotypes. |
| |
Authors: | H Okuda S Hirai Y Takaki M Kamada M Baba N Sakai T Kishida S Kaneko M Yao S Ohno T Shuin |
| |
Affiliation: | Department of Urology, Kochi Medical School, Kochi, 783-8505, Japan. |
| |
Abstract: | VHL tumor suppressor protein contains two domains, alpha and beta. The alpha-domain is involved in the formation of a large protein complex suggested to be involved in ubiquitin-mediated protein degradation. However, the role of the beta-domain, which may recognize the target proteins for protein degradation, remains unknown. Here we report that the beta-domain interacts directly with atypical PKC isotypes, PKCzeta and PKClambda. Further, the regulatory domain of aPKC is sufficient for this direct protein-protein interaction. Since aPKC isotypes have been implicated in the regulation of cell growth and apoptosis, these results suggest that aPKC isotypes are potential direct target of the VHL beta-domain. |
| |
Keywords: | |
|
|