A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4

被引:51
作者
Martinez-Noel, G
Niedenthal, R
Tamura, T
Harbers, K
机构
[1] Univ Hamburg, Heinrich Pette Inst Expt Virol & Immunol, D-20251 Hamburg, Germany
[2] Med Hsch Hannover, Inst Physiol Chem, D-30623 Hannover, Germany
关键词
ubiquitin-conjugating enzyme; RING finger protein; protein-protein interaction;
D O I
10.1016/S0014-5793(99)00823-6
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
The ubiquitin-conjugating enzyme UbcM4 was previously shown to be necessary for normal mouse development. As a first step in identifying target proteins or proteins involved in the specificity of UbcM4-mediated ubiquitylation, we have isolated seven cDNAs encoding proteins that specifically interact with UbcM4 but with none of the other Ubcs tested. This interaction was observed in yeast as well as in mammalian cells. With one exception, all UbcM4-interacting proteins (UIPs) belong to a family of proteins that contain a RING finger motif. As they are structurally related to RING finger proteins that have recently been shown to play an essential role in protein ubiquitylation and degradation, the possibility is discussed that UIPs are involved in the specific recognition of substrate proteins of UbcM4. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:257 / 261
页数:5
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