Direct interaction of the β-domain of VHL tumor suppressor protein with the regulatory domain of atypical PKC isotypes

被引：76

作者：

Okuda, H

Hirai, S

Takaki, Y

Kamada, M

Baba, M

Sakai, N

Kishida, T

Kaneko, S

Yao, M

Ohno, S ^{[1
]}

Shuin, T

机构：

[1] Kochi Med Sch, Dept Urol, Kochi 7838505, Japan

[2] Yokohama City Univ, Sch Med, Dept Mol Biol, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan

[3] Yokohama City Univ, Sch Med, Dept Urol, Kanazawa Ku, Yokohama, Kanagawa 2360004, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1999年 / 263卷 / 02期

关键词：

D O I：

10.1006/bbrc.1999.1347

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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, PKC zeta and PKC lambda. 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. (C) 1999 Academic Press.

引用

页码：491 / 497

页数：7

共 42 条

[1] Atypical protein kinase Cλ binds and regulates p70 S6 kinase [J].