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F-box protein 4

Fbx4, F-box protein FBX4
This gene encodes a member of the F-box protein family which is characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into 3 classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene belongs to the Fbxs class. Alternative splicing of this gene generates 2 transcript variants. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, PCNA, SCF, Cullin, TRF1
Papers using Fbx4 antibodies
Phosphorylation by Akt1 promotes cytoplasmic localization of Skp2 and impairs APCCdh1-mediated Skp2 destruction
Supplier
Kyprianou Natasha, In PLoS ONE, 2008
... Rabbit antibodies: Emi1, Millipore; Fbx4, Rockland (Gilbertsville, PA); Fbx7, Fbx31, ...
Papers on Fbx4
Maintaining glycogen synthase kinase-3 activity is critical for mTOR kinase inhibitors to inhibit cancer cell growth.
New
Sun et al., Atlanta, United States. In Cancer Res, Jun 2014
Silencing expression of the ubiquitin E3 ligase FBX4 rescued this reduction, implicating FBX4 in mediating this effect of mTOR inhibition.
Alternative splicing variants of human Fbx4 disturb cyclin D1 proteolysis in human cancer.
New
Lu et al., Beijing, China. In Biochem Biophys Res Commun, May 2014
Fbx4 is a specific substrate recognition component of SCF ubiquitin ligases that catalyzes the ubiquitination and subsequent degradation of cyclin D1 and Trx1.
The splicing factor U2AF65 stabilizes TRF1 protein by inhibiting its ubiquitin-dependent proteolysis.
New
Chung et al., Seoul, South Korea. In Biochem Biophys Res Commun, Feb 2014
We also found that U2AF65 interferes with the interaction between TRF1 and Fbx4, an E3 ubiquitin ligase for TRF1.
The F-box protein β-TrCP promotes ubiquitination of TRF1 and regulates the ALT-associated PML bodies formation in U2OS cells.
New
Huang et al., Zhengzhou, China. In Biochem Biophys Res Commun, Jun 2013
It was reported that TRF1 can be degraded by the ubiquitin-proteasome pathway, involving in two regulation factors, Fbx4 and RLIM.
PP2A(Cdc55) regulates G1 cyclin stability.
New
Nickels et al., United States. In Cell Cycle, May 2013
D1 cyclin protein stability is regulated through its ubiquitylation and resulting proteolysis catalyzed by the SCF E3 ubiquitin ligase complex containing the F-box protein, Fbx4.
Computationally designed peptide inhibitors of the ubiquitin E3 ligase SCF(Fbx4).
New
Liu et al., Boulder, United States. In Chembiochem, Apr 2013
A structure-based computational approach was used to rationally design peptide inhibitors that can target an E3 ligase (SCF(Fbx4) )-substrate (TRF1) interface and subsequent ubiquitylation.
Multiplex mutation screening by mass spectrometry in gastrointestinal stromal tumours.
Kim et al., Seoul, South Korea. In Pathology, 2012
A substitution in FBX4 exon 1 (S8R), representing a germline single-nucleotide polymorphism, was observed in a case with KIT exon 11 missense mutation.
The Fbx4 tumor suppressor regulates cyclin D1 accumulation and prevents neoplastic transformation.
GeneRIF
Diehl et al., Philadelphia, United States. In Mol Cell Biol, 2011
Fbx4 expression is essential for cell homeostasis in somatic cells. Fbx4 ablation predisposes mice to multiple tumor phenotypes, with concomitant cyclin D1 deregulation and nuclear accumulation
Phosphorylation-dependent regulation of SCF(Fbx4) dimerization and activity involves a novel component, 14-3-3ɛ.
GeneRIF
Diehl et al., Philadelphia, United States. In Oncogene, 2011
14-3-3varepsilon binds to Ser12-phosphorylated Fbx4 to mediate dimerization and function.
Immunohistochemical and molecular markers in breast phyllodes tumors.
Troxell et al., Portland, United States. In Appl Immunohistochem Mol Morphol, 2011
Mutational analysis revealed an S8R substitution in FBX4 (an E3 ubiquitin ligase) in 3 cases: 1 benign and 2 borderline.
The influence of surface microroughness and hydrophilicity of titanium on the up-regulation of TGFβ/BMP signalling in osteoblasts.
Ivanovski et al., Gold Coast, Australia. In Biomaterials, 2011
Several other genes associated with the functionally important mechanisms relevant to bone healing, such as Wnt signalling (CTNNA1, FBX4, FZD6), angiogenesis (KDR), osteoclastogenesis (HSF2, MCL1) and proteolysis (HEXB, TPP1), were also differentially regulated.
Nuclear cyclin D1/CDK4 kinase regulates CUL4 expression and triggers neoplastic growth via activation of the PRMT5 methyltransferase.
Impact
Diehl et al., Philadelphia, United States. In Cancer Cell, 2010
Importantly, human cancers harboring mutations in Fbx4, the cyclin D1 E3 ligase, exhibit nuclear cyclin D1 accumulation and increased PRMT5 activity.
Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase.
GeneRIF
Hao et al., Farmington, United States. In J Biol Chem, 2010
Biochemical studies indicate that both the N-terminal domain and a loop connecting the linker and C-terminal domain of Fbx4 are critical for the dimerization and activation of the protein.
Structural basis of selective ubiquitination of TRF1 by SCFFbx4.
GeneRIF
Lei et al., Ann Arbor, United States. In Dev Cell, 2010
results reveal an atypical small GTPase domain within Fbx4 as a substrate-binding motif for SCF(Fbx4) and uncover a mechanism for selective ubiquitination and degradation of TRF1 in telomere homeostasis control
Lysine 269 is essential for cyclin D1 ubiquitylation by the SCF(Fbx4/alphaB-crystallin) ligase and subsequent proteasome-dependent degradation.
GeneRIF
Diehl et al., Philadelphia, United States. In Oncogene, 2010
Lysine 269 is essential for cyclin D1 ubiquitylation by the SCF(Fbx4/alphaB-crystallin) ligase.
SCF(Fbx4/alphaB-crystallin) E3 ligase: when one is not enough.
Review
Diehl et al., Philadelphia, United States. In Cell Cycle, 2008
Cyclin D1 proteolysis requires phosphorylation by GSK3beta at Thr-286; additional work recently established that p286-D1 is a substrate for the SCF(Fbx4/alphaB-crystallin) E3 ligase.
Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer.
Impact
GeneRIF
Diehl et al., Philadelphia, United States. In Cancer Cell, 2008
Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer.
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