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F-box and leucine-rich repeat protein 4

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 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 Fbls class and, in addition to an F-box, contains at least 9 tandem leucine-rich repeats. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, AGE, FKBP51, Scratch, PDGF-C
Papers on Fbxl4
Detailed Biochemical and Bioenergetic Characterization of FBXL4-Related Encephalomyopathic Mitochondrial DNA Depletion.
Lines et al., Ottawa, Canada. In Jimd Rep, Oct 2015
UNASSIGNED: Mutations of FBXL4, which encodes an orphan mitochondrial F-box protein, are a recently identified cause of encephalomyopathic mtDNA depletion.
Characterization of the platelet transcriptome by RNA sequencing in patients with acute myocardial infarction.
Johnson et al., Framingham, United States. In Platelets, Oct 2015
Several transcripts displayed suggestively higher (FBXL4, ECHDC3, KCNE1, TAOK2, AURKB, ERG, and FKBP5) and lower (MIAT, PVRL3, and PZP) expression in STEMI platelets compared to NSTEMI.
Clinical, morphological, biochemical, imaging and outcome parameters in 21 individuals with mitochondrial maintenance defect related to FBXL4 mutations.
McFarland et al., Bregenz, Austria. In J Inherit Metab Dis, Sep 2015
FBXL4 deficiency is a recently described disorder of mitochondrial maintenance associated with a loss of mitochondrial DNA in cells.
Whole exome sequencing of suspected mitochondrial patients in clinical practice.
Rodenburg et al., Nijmegen, Netherlands. In J Inherit Metab Dis, May 2015
TUFM, MTFMT, FBXL4), in the subgroup of patients with the lowest suspicion for a mitochondrial disorder we found mutations in several genes associated with neuromuscular disorders (e.g.
FBXL5 inhibits metastasis of gastric cancer through suppressing Snail1.
Zhang et al., Shanghai, China. In Cell Physiol Biochem, 2014
However, a role of FBXL4 in regulation of other EMT-associated proteins is not unknown.
Mutations in FBXL4, encoding a mitochondrial protein, cause early-onset mitochondrial encephalomyopathy.
Zeviani et al., Maywood, United States. In Am J Hum Genet, 2013
Whole-exome sequencing and autozygosity mapping studies, independently performed in subjects with defective combined mitochondrial OXPHOS-enzyme deficiencies, identified a total of nine disease-segregating FBXL4 mutations in seven unrelated mitochondrial disease families, composed of six singletons and three siblings.
Mutations in FBXL4 cause mitochondrial encephalopathy and a disorder of mitochondrial DNA maintenance.
Taylor et al., Houston, United States. In Am J Hum Genet, 2013
Through whole-exome sequencing, we identified recessive nonsense and splicing mutations in FBXL4 segregating in three unrelated consanguineous kindreds in which affected children present with a fatal encephalopathy, lactic acidosis, and severe mtDNA depletion in muscle.
The SKP1-Cul1-F-box and leucine-rich repeat protein 4 (SCF-FbxL4) ubiquitin ligase regulates lysine demethylase 4A (KDM4A)/Jumonji domain-containing 2A (JMJD2A) protein.
Whetstine et al., United States. In J Biol Chem, 2011
SKP1-Cul1-F-box and leucine-rich repeat protein 4 (SCF-FbxL4) ubiquitin ligase regulates lysine demethylase 4A (KDM4A)/Jumonji domain-containing 2A (JMJD2A) protein
Expression and SNP association analysis of porcine FBXL4 gene.
Peng et al., Beijing, China. In Mol Biol Rep, 2010
As a kind of E3 ligase, the product of FBXL4 gene belongs to a member of FBLs which is the biggest eukaryotic subfamily of F-BOX proteins, it can recognize some substrate through particular protein-protein interaction domains.
The fly CAMTA transcription factor potentiates deactivation of rhodopsin, a G protein-coupled light receptor.
Li et al., Worcester, United States. In Cell, 2006
Our data suggest that calmodulin/CAMTA/Fbxl4 may mediate a long-term feedback regulation of the activity of Ca(2+)-stimulating GPCRs, which could prevent cell damage due to extra Ca(2+) influx.
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