F-box protein

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F-box linker domain
PDB 1fs2 EBI.jpg
Structure of the LRR linker domain of Skp2 in the Skp1-Skp2 complex. [1]
Identifiers
SymbolF-box
Pfam PF00646
Pfam clan CL0271
InterPro IPR001810
SMART SM00256
PROSITE PS50181
SCOP2 1fs2 / SCOPe / SUPFAM
Membranome 630
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

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 26S proteasome.

Contents

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. [2] The F-box motif of Skp2, consisting of three alpha-helices, interacts directly with the SCF protein Skp1. [2] 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. [3]

Function

F-box proteins have also been associated with cellular functions such as signal transduction and regulation of the cell cycle. [4] In plants, many F-box proteins are represented in gene networks broadly regulated by microRNA-mediated gene silencing via RNA interference. [5] 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. [6] ACRE189/ACIF1 can regulate cell death and defense when the pathogen is recognized in the Tobacco and Tomato plant. [7]

In human cells, under high-iron conditions, two iron atoms stabilise the F-Box FBXL5 and then the complex mediates the ubiquitination of IRP2. [8]

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. [9]

References

  1. ↑ Schulman BA, Carrano AC, Jeffrey PD, et al. (November 2000). "Insights into SCF ubiquitin ligases from the structure of the Skp1-Skp2 complex". Nature. 408 (6810): 381–6. Bibcode:2000Natur.408..381S. doi:10.1038/35042620. PMID   11099048. S2CID   4300503.
  2. 1 2 Bai C, Sen P, Hofmann K, Ma L, Goebl M, Harper JW, et al. (1996). "SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box". Cell. 86 (2): 263–274. doi:10.1016/S0092-8674(00)80098-7. PMID   8706131.
  3. ↑ Kipreos ET, Pagano M (2000). "The F-box protein family". Genome Biol. 1 (5) REVIEWS3002. doi: 10.1186/gb-2000-1-5-reviews3002 . PMC   138887 . PMID   11178263.
  4. ↑ Craig KL, Tyers M (1999). "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. doi: 10.1016/S0079-6107(99)00010-3 . PMID   10581972.
  5. ↑ Jones-Rhoades MW, Bartel DP, Bartel B (2006). "MicroRNAS and their regulatory roles in plants". Annu Rev Plant Biol. 57 (1): 19–53. Bibcode:2006AnRPB..57...19J. doi:10.1146/annurev.arplant.57.032905.105218. PMID   16669754.
  6. ↑ Peng J, Yu D, Wang L, Xie M, Yuan C, Wang Y, et al. (2012). "Arabidopsis F-box gene FOA1 involved in ABA signaling". Science China Life Sciences. 55 (6): 497–506. doi:10.1007/s11427-012-4332-9. PMID   22744179.
  7. ↑ Ha VD, Tsitsigiannis DI, Rowland O, Lo J, Rallapalli G, Maclean D, et al. (2008). "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. Bibcode:2008PlanC..20..697V. doi:10.1105/tpc.107.056978.
  8. ↑ Moroishi T, Nishiyama M, Takeda Y, Iwai K, Nakayama KI (2011). "The FBXL5-IRP2 axis is integral to control of iron metabolism in vivo". Cell Metabolism. 14 (3): 339–351. doi:10.1016/j.cmet.2011.07.011. PMID   21907140.
  9. ↑ Kaiser P, Su NY, Yen JL, Ouni I, Flick K (2006). "The yeast ubiquitin ligase SCFMet30: connecting environmental and intracellular conditions to cell division". Cell Division. 1: 16. doi: 10.1186/1747-1028-1-16 .

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