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Degradation of the cyclin‐dependent kinase inhibitor KRP1 is regulated by two different ubiquitin E3 ligases
Author(s) -
Ren Hong,
Santner Aaron,
Pozo Juan Carlos del,
Murray James A. H.,
Estelle Mark
Publication year - 2008
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/j.1365-313x.2007.03370.x
Subject(s) - ubiquitin , f box protein , microbiology and biotechnology , cell cycle , cyclin dependent kinase complex , biology , ubiquitin ligase , cyclin dependent kinase , proteasome , cell division control protein 4 , skp2 , protein degradation , cyclin a , protein kinase a , ubiquitin conjugating enzyme , cyclin , kinase , cyclin dependent kinase 3 , cyclin dependent kinase 2 , biochemistry , cell , gene
Summary In animals and fungi, a group of proteins called the cyclin‐dependent kinase inhibitors play a key role in cell cycle regulation. However, comparatively little is known about the role of these proteins in plant cell cycle regulation. To gain insight into the mechanisms by which the plant cell cycle is regulated, we studied the cyclin‐dependent kinase inhibitor KRP1 in Arabidopsis. KRP1 interacts with the CDKA;1/CYCD2;1 complex in planta and functions in the G1–S transition of the cell cycle. Furthermore, we show that KRP1 is a likely target of the ubiquitin/proteasome pathway. Two different ubiquitin protein ligases, SCF SKP2 and the RING protein RKP, contribute to its degradation. These results suggest that SCF SKP2b and RPK play an important role in the cell cycle through regulating KRP1 protein turnover.