The F-box protein family.
The F-box protein family.
复制标题
F-box蛋白家族。
DOI:
10.1186/gb-2000-1-5-reviews3002
复制
发表时间:
2000
期刊:
影响因子:
12.3
通讯作者:
Pagano, M
中科院分区:
文献类型:
--
作者:
Kipreos, E T;Pagano, M
F-box proteins were first described as components of ubiquitin ligase complexes, but have more recently been found to be involved in a variety of cellular functions, including in the kinetochore and in translational elongation. 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.