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Plants respond to gibberellins via GID1-dependent degradation of DELLA proteins. Here, Nemoto et al. show that the gibberellin response is positively regulated by tyrosine phosphorylation of GARU, an E3 ubiquitin ligase that mediates degradation of GID1.
The sorting of soluble proteins for degradation in the vacuole is of vital importance in plant cells, and relies on the activity of vacuolar sorting receptors (VSRs). Laboratory experiments with tobacco mesophyll protoplasts suggest that VSRs are required for the transport of ligands from the endoplasmic reticulum and Golgi to the trans-Golgi network/early endosome.
Cold stress activates Arabidopsis thaliana plasma membrane-localized CRPK1, which leads to 14-3-3 proteins entering the nucleus and promoting the degradation of CBF transcription factors, thus attenuating the cold-induced response.
The auxin receptor TIR1 is an F-box protein functioning in a ubiquitin ligase complex to target repressors for degradation. It is itself an unstable protein, but newly identified mutations protect both TIR1 and its substrates
from degradation. These mutations could help in identifying the substrates for hundreds of other F-box proteins.