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Gene Review

FBXO2  -  F-box protein 2

Homo sapiens

Synonyms: F-box only protein 2, FBG1, FBX2, Fbg1, Fbs1, ...
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Disease relevance of FBXO2


High impact information on FBXO2

  • Pre-integrin beta 1 is a target of Fbx2; these two proteins interact in the cytosol after inhibition of the proteasome [4].
  • In addition, expression of the mutant Fbx2 Delta F, which lacks the F-box domain that is essential for forming the SCF complex, appreciably blocks degradation of typical substrates of the ER-associated degradation pathway [4].
  • CHIP facilitates the ubiquitination and degradation of Fbx2-bound glycoproteins, including unassembled NMDA receptor subunits [5].
  • These findings indicate that CHIP acts with Fbx2 in a novel ubiquitination pathway that links CHIP to glycoprotein quality control in neurons [5].
  • Here we show that Fbx2, a brain-enriched F-box protein implicated in the ubiquitination of glycoproteins discarded from the endoplasmic reticulum, binds the co-chaperone/ubiquitin ligase CHIP (C terminus of Hsc-70-interacting protein) through a unique N-terminal PEST domain in Fbx2 [5].

Biological context of FBXO2

  • The presence of an F box in NFB42 suggests that it may be involved in cell cycle regulation; however, its expression in postmitotic neurons indicates that it is not involved in regulating typical cell cycle events [2].
  • In addition, we have evaluated the effect of hFbg on two functional events related to expression and resolution of inflammation: cytotoxic capacity and rate of neutrophil apoptosis [6].
  • Ectopic expression of NFB42 both suppressed the formation of aggresome-like structures and the phosphorylation of the translational regulator eIF2alpha induced by overproduction of SHPS-1 as well as increased the amount of mature SHPS-1 at the cell surface [7].

Anatomical context of FBXO2

  • The expression of full-length NFB42, but not an F box deletion mutant, inhibits proliferation in both cell lines [2].
  • We have now shown that incubation of purified neutrophils with hFbg induces a transient and rapid elevation of free intracellular Ca2+ [6].

Associations of FBXO2 with chemical compounds

  • These analyses revealed that Man(3)GlcNAc(2) had the strongest affinity and the chitobiose and alpha1-->6 linked Man residue are necessary for Fbs1 to recognize a sugar [8].

Other interactions of FBXO2

  • Although OCP1 displays extensive homology to an F-box protein recently cloned from rat brain (NFB42), clustered sequence non-identities indicate that the two proteins are transcribed from distinct genes [9].


  1. Replication-initiator protein (UL9) of the herpes simplex virus 1 binds NFB42 and is degraded via the ubiquitin-proteasome pathway. Eom, C.Y., Lehman, I.R. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  2. A novel F box protein, NFB42, is highly enriched in neurons and induces growth arrest. Erhardt, J.A., Hynicka, W., DiBenedetto, A., Shen, N., Stone, N., Paulson, H., Pittman, R.N. J. Biol. Chem. (1998) [Pubmed]
  3. The neural F-box protein NFB42 mediates the nuclear export of the herpes simplex virus type 1 replication initiator protein (UL9 protein) after viral infection. Eom, C.Y., Heo, W.D., Craske, M.L., Meyer, T., Lehman, I.R. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  4. E3 ubiquitin ligase that recognizes sugar chains. Yoshida, Y., Chiba, T., Tokunaga, F., Kawasaki, H., Iwai, K., Suzuki, T., Ito, Y., Matsuoka, K., Yoshida, M., Tanaka, K., Tai, T. Nature (2002) [Pubmed]
  5. A novel route for F-box protein-mediated ubiquitination links CHIP to glycoprotein quality control. Nelson, R.F., Glenn, K.A., Miller, V.M., Wen, H., Paulson, H.L. J. Biol. Chem. (2006) [Pubmed]
  6. Fibrinogen promotes neutrophil activation and delays apoptosis. Rubel, C., Fernández, G.C., Dran, G., Bompadre, M.B., Isturiz, M.A., Palermo, M.S. J. Immunol. (2001) [Pubmed]
  7. Ubiquitination-mediated regulation of biosynthesis of the adhesion receptor SHPS-1 in response to endoplasmic reticulum stress. Murai-Takebe, R., Noguchi, T., Ogura, T., Mikami, T., Yanagi, K., Inagaki, K., Ohnishi, H., Matozaki, T., Kasuga, M. J. Biol. Chem. (2004) [Pubmed]
  8. Thermodynamic analysis of interactions between N-linked sugar chains and F-box protein Fbs1. Hagihara, S., Totani, K., Matsuo, I., Ito, Y. J. Med. Chem. (2005) [Pubmed]
  9. OCP1, an F-box protein, co-localizes with OCP2/SKP1 in the cochlear epithelial gap junction region. Henzl, M.T., O'Neal, J., Killick, R., Thalmann, I., Thalmann, R. Hear. Res. (2001) [Pubmed]
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