Biology:F-box protein
| F-box linker domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 | |||||||||
| Identifiers | |||||||||
| Symbol | F-box | ||||||||
| Pfam | PF00646 | ||||||||
| Pfam clan | CL0271 | ||||||||
| InterPro | IPR001810 | ||||||||
| SMART | SM00256 | ||||||||
| PROSITE | PS50181 | ||||||||
| SCOP2 | 1fs2 / SCOPe / SUPFAM | ||||||||
| Membranome | 630 | ||||||||
| |||||||||
F-box proteins, sometimes abbreviated as FBX,[1][2] 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 26S proteasome.
Core components
F-box domain is a protein structural motif of about 50 amino acids that mediates protein–protein interactions. It has consensus sequence and varies in few positions. It was first identified in cyclin F.[3] The F-box motif of Skp2, consisting of three alpha-helices, interacts directly with the SCF protein Skp1.[3] F-box domains commonly exist in proteins in cancer with other protein–protein interaction motifs such as leucine-rich repeats (illustrated in the Figure) and WD repeats, which are thought to mediate interactions with SCF substrates.[4]
Function
F-box proteins have also been associated with cellular functions such as signal transduction and regulation of the cell cycle.[5] In plants, many F-box proteins are represented in gene networks broadly regulated by microRNA-mediated gene silencing via RNA interference.[6] F-box proteins are involved in many plant vegetative and reproduction growth and development. For example, F-box protein-FOA1 involved in abscisic acid (ABA) signaling to affect the seed germination.[7] ACRE189/ACIF1 can regulate cell death and defense when the pathogen is recognized in the Tobacco and Tomato plant.[8]
In human cells, under high-iron conditions, two iron atoms stabilise the F-Box FBXL5 and then the complex mediates the ubiquitination of IRP2.[9]
Regulation
F-box protein levels can be regulated by different mechanisms. The regulation can occur via protein degradation process and association with SCF complex . For example, in yeast, the F-box protein Met30 can be ubiquitinated in a cullin-dependent manner.[10]
References
- ↑ Hua, Zhihua; Zou, Cheng; Shiu, Shin-Han; Vierstra, Richard D. (2011-01-28). "Phylogenetic Comparison of F-Box (FBX) Gene Superfamily within the Plant Kingdom Reveals Divergent Evolutionary Histories Indicative of Genomic Drift" (in en). PLOS ONE 6 (1). doi:10.1371/journal.pone.0016219. ISSN 1932-6203. PMID 21297981. Bibcode: 2011PLoSO...616219H.
- ↑ Kuroda, Hirofumi; Yanagawa, Yuki; Takahashi, Naoki; Horii, Yoko; Matsui, Minami (2012-11-15). "A Comprehensive Analysis of Interaction and Localization of Arabidopsis SKP1-LIKE (ASK) and F-Box (FBX) Proteins" (in en). PLOS ONE 7 (11). doi:10.1371/journal.pone.0050009. ISSN 1932-6203. PMID 23166809. Bibcode: 2012PLoSO...750009K.
- ↑ 3.0 3.1 "SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box". Cell 86 (2): 263–274. 1996. doi:10.1016/S0092-8674(00)80098-7. PMID 8706131.
- ↑ "The F-box protein family". Genome Biol. 1 (5). 2000. doi:10.1186/gb-2000-1-5-reviews3002. PMID 11178263.
- ↑ "The F-box: a new motif for ubiquitin dependent proteolysis in cell cycle regulation and signal transduction". Prog. Biophys. Mol. Biol. 72 (3): 299–328. 1999. doi:10.1016/S0079-6107(99)00010-3. PMID 10581972.
- ↑ "MicroRNAS and their regulatory roles in plants". Annu Rev Plant Biol 57 (1): 19–53. 2006. doi:10.1146/annurev.arplant.57.032905.105218. PMID 16669754. Bibcode: 2006AnRPB..57...19J.
- ↑ "Arabidopsis F-box gene FOA1 involved in ABA signaling". Science China Life Sciences 55 (6): 497–506. 2012. doi:10.1007/s11427-012-4332-9. PMID 22744179.
- ↑ "The F-box protein ACRE189/ACIF1 regulates cell death and defense responses activated during pathogen recognition in tobacco and tomato". Plant Cell 20 (3): 697–719. 2008. doi:10.1105/tpc.107.056978. PMID 18375657. Bibcode: 2008PlanC..20..697V.
- ↑ "The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo". Cell Metabolism 14 (3): 339–351. 2011. doi:10.1016/j.cmet.2011.07.011. PMID 21907140.
- ↑ "The yeast ubiquitin ligase SCFMet30: connecting environmental and intracellular conditions to cell division". Cell Division 1: 16. 2006. doi:10.1186/1747-1028-1-16. PMID 16895602.
Further reading
- "F-box proteins: the key to protein degradation.". J Biomed Sci 13 (2): 181–91. 2006. doi:10.1007/s11373-005-9058-2. PMID 16463014.
External links
- F-Box+Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)
- F-box+motifs at the US National Library of Medicine Medical Subject Headings (MeSH)
 |  |
