A role for the ubiquitin–26S-proteasome pathway in gibberellin signaling

• Published in: Trends in plant science Vol. 8; no. 10; pp. 492 - 497
• Main Authors: Itoh, Hironori, Matsuoka, Makoto, Steber, Camille M.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 01.10.2003; Elsevier
• Subjects: Amino Acid Sequence; Biological and medical sciences; Cell physiology; Fundamental and applied biological sciences. Psychology; Gibberellins - metabolism; Molecular and cellular biology; Molecular Sequence Data; Peptide Hydrolases - metabolism; Plants - genetics; Plants - metabolism; Proteasome Endopeptidase Complex; Sequence Alignment; Sequence Homology, Amino Acid; Signal transduction; Signal Transduction - physiology; Transcription Factors - metabolism; Ubiquitin - metabolism; Multicatalytic endopeptidase complex; Enzyme; Gibberellin; Review; Arabidopsis thaliana; Peptidases; Signal transduction; Cruciferae; Proteolysis; Dicotyledones; Angiospermae; Hydrolases; Spermatophyta; Mutation
• ISSN: 1360-1385; 1878-4372
• DOI: 10.1016/j.tplants.2003.08.002

The gibberellin (GA) signaling pathway, like auxin and jasmonate signaling, uses the ubiquitin–proteasome pathway to control expression through protein degradation. A conserved F-box protein of an SCF E3 ubiquitin ligase is a positive regulator of GA signaling in Arabidopsis and rice. GA apparently stimulates stem elongation by causing this SCF complex to regulate negatively a family of negative regulators of GA response (the DELLA family of putative transcription factors). The DELLA family members AtRGA or (Repressor of ga1-3) and OsSLR1 (SLENDER RICE1) proteins both appear to be subject to GA-induced proteolysis. The need to have the F-box genes AtSLY1 and OsGID2 for this proteolysis suggests that GA causes proteolysis of AtRGA/OsSLR1 via the SCF AtSLY1/OsGID2 ubiquitin ligase.