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Protein family review

The F-box protein family

Edward T Kipreos1 and Michele Pagano2

Author Affiliations

1 Department of Cellular Biology, University of Georgia, Athens, GA 30602, USA

2 Department of Pathology, New York University School of Medicine, New York, NY 10016, USA

Genome Biology 2000, 1:reviews3002-reviews3002.7  doi:10.1186/gb-2000-1-5-reviews3002

Published: 10 November 2000

Abstract

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.