Modulation of sensitivity and selectivity in plant signaling by proteasomal destabilization.

The ubiquitin (Ub) system of intracellular protein degradation regulates the abundance of numerous proteins that control plant growth and development. Recent advances have begun to illustrate how environmental and endogenous signals affect plant responses through Ub-related proteolysis, the importance of combinatorial control in regulated protein destruction and how multiprotein complexes confer sensitivity and selectivity to ubiquitination. Further insight into the cell biology of Ub-chain assembly and proteasomal degradation, as well as into the relationship between proteolysis and other regulatory modifications, will be essential for understanding the mechanistic basis of the integration of diverse plant signals.