RING finger specificity in SCF-driven protein destruction.
SCF ubiquitin ligases contain an E3 core composed of Skp1, Cul1, a member of the Rbx1/Roc1 family of RING finger proteins, and a modular F box protein that functions in substrate targeting. Work published in this issue of Developmental Cell indicates that distinct Rbx1/Roc1 family members are used to control ubiquitination of distinct targets, suggesting that the RING finger subunit may contribute to ubiquitination specificity.
Jin
Jianping
J
Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, Texas 77030, USA.
Harper
J Wade
JW
D000818:Animals; D004330:Drosophila / Q000196:embryology / Q000235:genetics / Q000378:metabolism*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism; D004789:Enzyme Activation; D008025:Ligases / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D010453:Peptide Synthases / Q000737:chemistry / Q000378:metabolism*; D010802:Phylogeny; D011994:Recombinant Proteins / Q000378:metabolism; D044843:SKP Cullin F-Box Protein Ligases; D013379:Substrate Specificity; D044767:Ubiquitin-Protein Ligases; D014452:Ubiquitins / Q000378:metabolism
D029721:Drosophila Proteins; D011994:Recombinant Proteins; D014452:Ubiquitins; D044843:SKP Cullin F-Box Protein Ligases; D044767:Ubiquitin-Protein Ligases; D008025:Ligases; D010453:Peptide Synthases