Title |
F-box proteins: the key to protein degradation
|
---|---|
Published in |
Journal of Biomedical Science, February 2006
|
DOI | 10.1007/s11373-005-9058-2 |
Pubmed ID | |
Authors |
Margaret S. Ho, Pei-I Tsai, Cheng-Ting Chien |
Abstract |
The eukaryotic protein degradation pathway involves the ubiquitin (Ub) modification of substrates targeted for degradation by the 26S proteasome. The addition of Ub, a process called ubiquitination, is mediated by enzymes including the E3 Ub ligases which transfer the Ub to targeted substrates. A major type of E3 Ub ligases, the SCF (Skp-Cullin-F-box) complex, is composed of four major components: Skp1, Cul1/Cdc53, Roc1/Rbx1/Hrt1, and an F-box protein. The F-box component of the SCF machineries is responsible for recognizing different substrates for ubiquitination. Interaction with components of the SCF complex is mediated through the F-box motif of the F-box protein while it associates with phosphorylated substrates through its second protein-protein interaction motif such as Trp-Asp (WD) repeats or leucine-rich repeats (LRRs). By targeting diverse substrates, F-box proteins exert controls over stability of proteins and regulate the mechanisms for a wide-range of cellular processes. Here we discuss the importance of F-box proteins by providing a general overview and examples of how F-box proteins function in various cellular settings such as tissue development, cell proliferation, and cell death, in the modeling organism Drosophila. |
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Unknown | 141 | 96% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 23 | 16% |
Student > Master | 20 | 14% |
Student > Bachelor | 18 | 12% |
Professor > Associate Professor | 13 | 9% |
Other | 20 | 14% |
Unknown | 16 | 11% |
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Other | 14 | 10% |
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