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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

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)
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
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.
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.
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