Ubiquitin biology: an old dog learns an old trick.
Regulated protein degradation in eukaryotes occurs principally through covalent tagging of substrates with ubiquitin, thereby targeting them for destruction by 26S proteasomes. Classical allostery has now been added to the repertoire of mechanisms that can modulate ubiquitin tagging, allowing feed-forward regulation to be achieved through targeted protein destruction.
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D000494:Allosteric Regulation; D004151:Dipeptides / Q000378:metabolism; D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism*; D018398:Homeodomain Proteins / Q000235:genetics / Q000378:metabolism; D008025:Ligases; D010447:Peptide Hydrolases / Q000378:metabolism*; D046988:Proteasome Endopeptidase Complex; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins; D013379:Substrate Specificity; D014157:Transcription Factors / Q000235:genetics / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases; D014452:Ubiquitins / Q000378:metabolism*
C090457:CUP9 protein, S cerevisiae; D004151:Dipeptides; D005656:Fungal Proteins; D018398:Homeodomain Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D014452:Ubiquitins; C066066:UBR1 protein, S cerevisiae; D044767:Ubiquitin-Protein Ligases; D010447:Peptide Hydrolases; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease; D008025:Ligases