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F-box proteins : ウィキペディア英語版
F-box protein

F-box proteins are proteins containing at least one F-box domain. The first identified F-box protein is one of three components of the SCF complex, which mediates ubiquitination of proteins targeted for degradation by the proteasome.
F-box proteins have also been associated with cellular functions such as signal transduction and regulation of the cell cycle. In plants, many F-box proteins are represented in gene networks broadly regulated by microRNA-mediated gene silencing via RNA interference.
In human cells, in high-iron condition, two iron atoms stabilise the F-Box FBXL5 and then the complex mediates the ubiquitination of IRP2.
The F-box domain is a protein structural motif of about 50 amino acids that mediates protein–protein interactions. It was first identified in cyclin F.
The F-box motif interacts directly with the SCF protein Skp1, and F-box domains commonly exist in proteins in concert with other protein–protein interaction motifs such as leucine-rich repeats and WD repeats, which are thought to mediate interactions with SCF substrates.
==References==


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