SCF Regulates Root Quiescent Center Cell Division via Protein Degradation of APC/C.

Homeostatic regulation of meristematic stem cells accomplished by maintaining a balance between stem cell self-renewal and differentiation is critical for proper plant growth and development. The quiescent center (QC) regulates root apical meristem homeostasis by maintaining stem cell fate during plant root development. Cell cycle checkpoints, such as anaphase promoting complex/cyclosome/CELL CYCLE SWITCH 52 A2 (APC/C), strictly control the low proliferation rate of QC cells. Although APC/C plays a critical role in maintaining QC cell division, the molecular mechanism that regulates its activity remains largely unknown. Here, we identified SCF, a ubiquitin E3 ligase, as a key regulator of QC cell division through the direct proteolysis of CCS52A2. FBS1 activity is positively associated with QC cell division and CCS52A2 proteolysis. overexpression or knockout consistently resulted in abnormal root development, characterized by root growth inhibition and low mitotic activity in the meristematic zone. Loss-of-function mutation of , on the other hand, resulted in low QC cell division, extremely low expression, and rapid root growth. The 26S proteasome-mediated degradation of CCS52A2 was facilitated by its direct interaction with F-box stress induced 1 (FBS1). The FBS1 genetically interacted with APC/C-ERF115-PSKR1 signaling module for QC division. Thus, our findings establish SCF-mediated CCS52A2 proteolysis as the molecular mechanism for controlling QC cell division in plants.