The F-box protein family

By E. Kipreos, M. Pagano. Genome Biology, 2000

722 citations recorded by the source corpus.

SummaryThe F-box is a protein motif of approximately 50 amino acids that functions as a site of protein-protein interaction. F-box proteins were first characterized as components of SCF ubiquitin-ligase complexes (named after their main components, Skp I, Cullin, and an F-box protein), in which they bind substrates for ubiquitin-mediated proteolysis. The F-box motif links the F-box protein to other components of the SCF complex by binding the core SCF component Skp I. F-box proteins have more recently been discovered to function in non-SCF protein complexes in a variety of cellular functions. There are 11 F-box proteins in budding yeast, 326 predicted in Caenorhabditis elegans, 22 in Drosophila, and at least 38 in humans. F-box proteins often include additional carboxy-terminal motifs capable of protein-protein interaction; the most common secondary motifs in yeast and human F-box proteins are WD repeats and leucine-rich repeats, both of which have been found to bind phosphorylated substrates to the SCF complex. The majority of F-box proteins have other associated motifs, and the functions of most of these proteins have not yet been defined.

Subfields: Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/741988991b95cf84bd968f0835cd4bfad1d2bc77

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In Cell Biology

1. J. Bartek
2. J. Lukas
3. C. Lukas
4. M. Pagano
5. T. Boller
6. J. Thorner
7. Cyril Zipfel
8. Raymond E. Chen

In Molecular Biology

1. J. Bartek
2. J. Lukas
3. Cyril Zipfel
4. C. Lukas
5. Jonathan D. G. Jones
6. T. Boller
7. L. Navarro
8. Stephen G Thomas

Citations in the corpus

• Structure of the Cul1–Rbx1–Skp1–F boxSkp2 SCF ubiquitin ligase complex (2002, background): “The large number of F-box proteins in eukaryotic genomes (at least 38 in huma”
• The Transcriptional Innate Immune Response to flg22. Interplay and Overlap with Avr Gene-Dependent Defense Responses and Bacterial Pathogenesis1[w] (2004, background): “F-box proteins are components of the E3-ligase SCF complex and are involved in the delivery of appropriate targets to this complex for ubiquitylation followed by degradation in the proteasome (Deshaies, 1999; Kipreos and Pagano, 2000).”
• Function and regulation in MAPK signaling pathways: lessons learned from the yeast Saccharomyces cerevisiae. (2007, background): “As expected, stimulation of Ste11 in the Sho1-dependent branch requires the function of Cdc42 and Ste20 [9,98,99].”
• Hormonal Control of the Plant Cell Cycle (2004, background): “In other organisms SCF complexes are involved in the action of cell cycle components such as yeast Cln1 and Cln2 cyclins, human cyclin E and mouse p27 CDK inhibitor (Kipreos and Pagano 2000).”
• The Arabidopsis F-Box Protein SLEEPY1 Targets Gibberellin Signaling Repressors for Gibberellin-Induced Degradation (2004, background): “In addition, the F-box protein recruits the targets via its C-terminal protein–protein interaction domain and provides the substrate specificity to the SCF E3 (Kipreos and Pagano, 2000).”
• Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity (2004, background): “Eukaryotic F-box domains are typically associated with other interaction domain”
• EIN3-dependent regulation of plant ethylene hormone signaling by two arabidopsis F box proteins: EBF1 and EBF2. (2003, background): “The F box sequences are boxed and the residues corresponding to the F box consensus sequence (Kipreos and Pagano, 2000) are indicated in red.”
• Checking on DNA damage in S phase (2004, background): “The F-box proteins comprise a large family of substrate-adaptor proteins that link the enzymatic core of the SCF ubiquitin ligase with its substrate”