Degradation of the cyclin-dependent kinase inhibitor KRP1 is regulated by two different ubiquitin E3 ligases

Hong Ren, Aaron Santner, Juan Carlos Del Pozo, James A H Murray, Mark Estelle

Research output: Contribution to journalArticlepeer-review

74 Scopus citations

Abstract

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, SCFSKP2 and the RING protein RKP, contribute to its degradation. These results suggest that SCFSKP2b and RPK play an important role in the cell cycle through regulating KRP1 protein turnover.

Original languageEnglish (US)
Pages (from-to)705-716
Number of pages12
JournalPlant Journal
Volume53
Issue number5
DOIs
StatePublished - Mar 2008

Keywords

  • Arabidopsis
  • Cell cycle
  • KRP ubiquitin

Fingerprint Dive into the research topics of 'Degradation of the cyclin-dependent kinase inhibitor KRP1 is regulated by two different ubiquitin E3 ligases'. Together they form a unique fingerprint.

Cite this