The F-box protein family.
The 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.
Kipreos
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Department of Cellular Biology, University of Georgia, Athens, GA 30602, USA. ekipreos@cb.uga.edu
Pagano
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D000818:Animals; D019143:Evolution, Molecular; D005786:Gene Expression Regulation; D016678:Genome; D006801:Humans; D010453:Peptide Synthases / Q000235:genetics* / Q000378:metabolism; D010766:Phosphorylation; D044843:SKP Cullin F-Box Protein Ligases
D044843:SKP Cullin F-Box Protein Ligases; D010453:Peptide Synthases