mirage

SCF SKP2B - AND KPC1-DEPENDENT DEGRADATION OF CYCLIN-DEPENDENT KINASE INHIBITOR KRP1 AND CELL CYCLE REGULATION IN ARABIDOPSIS THALIANA

DSpace/Manakin Repository

Show simple item record

dc.contributor.advisor Estelle, Mark en_US
dc.contributor.author Ren, Hong en_US
dc.date.accessioned 2010-05-24T15:08:54Z
dc.date.available 2027-01-24T16:08:54Z
dc.date.available 2010-05-29T16:28:51Z
dc.date.issued 2010-05-24T15:08:54Z
dc.date.submitted 2005 en_US
dc.identifier.uri http://hdl.handle.net/2022/7010
dc.description Thesis (PhD) - Indiana University, Molecular, Cellular, and Developmental Biology, 2005 en_US
dc.description.abstract In animals and fungi, cyclin-dependent kinase inhibitors play a key role in cell cycle regulation by inhibiting the activities of cyclin-dependent kinase/cyclin complexes. However, little is known about the role of this group of proteins in plant cell cycle regulation. To gain insight into the mechanisms by which the plant cell cycle is regulated, I studied the cyclin-dependent kinase inhibitor KRP1 in Arabidopsis. The role of KRP1 in pericycle activation during lateral root initiation and in cell cycle regulation and how ubiquitin-mediated protein degradation regulates KRP1 protein turnover were investigated. My results show that KRP1 plays an important role in the regulation of pericycle activation during lateral root initiation. KRP1 interacts with the CDKA;1/CYCD2;1 complex in planta and functions in the G1-S transition of the cell cycle. KRP1 is an unstable protein in planta and its degradation depends on the 26S proteasome. Further, an SCF complex composed of CUL1 and SKP2b regulates KRP1 degradation. These results suggest that SCF SKP2B targets KRP1 for degradation by the 26S proteasome to regulate the G1-S transition of the cell cycle. In addition to SCF SKP2B-mediated KRP1 degradation, KRP1 degradation is also regulated by the RING finger ubiquitin ligase KPC1. To further understand the mechanisms of KRP1 degradation and identify novel proteins that regulate KRP1 degradation, I performed a genetic screen for mutations that stabilize KRP1 protein. Three mutants called msk (mutant stabilizes KRP1) caused by a recessive mutation were identified. These three msk mutants define three distinct genetic loci. The results of these studies reveal a novel function of KRP1 in the regulation of pericycle activation during lateral root initiation and provide new insight into the mechanisms by which plant cell cycle is regulated by ubiquitin-mediated protein degradation. en_US
dc.language.iso EN en_US
dc.publisher [Bloomington, Ind.] : Indiana University en_US
dc.subject.classification Biology, Molecular en_US
dc.title SCF SKP2B - AND KPC1-DEPENDENT DEGRADATION OF CYCLIN-DEPENDENT KINASE INHIBITOR KRP1 AND CELL CYCLE REGULATION IN ARABIDOPSIS THALIANA en_US
dc.type Doctoral Dissertation en_US


Files in this item

This item appears in the following Collection(s)

Show simple item record

Search IUScholarWorks


Advanced Search

Browse

My Account

Statistics