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regulatory circuit involving FBXL5 and CIA (show ASF1A Proteins) acts through both IRPs to control iron metabolism and promote optimal cell growth
analysis of the redox sensing mechanism by which FBXL5 can serve as an iron metabolism regulator within mammalian cells
FBXL5 regulates cortactin (show CTTN Proteins) through induction of its ubiquitylation, and FBXL5 similarly regulates Snail1 (show SNAI1 Proteins).
FBXL5-mediated degradation of CITED2 (show CITED2 Proteins) leads to the activation of HIF-1alpha (show HIF1A Proteins).
results thus suggest that HERC2 regulates the basal turnover of FBXL5, and that this ubiquitin-dependent degradation pathway contributes to the control of mammalian iron metabolism
F-box and leucine-rich repeat protein 5 (FBXL5) is required for maintenance of cellular and systemic iron homeostasis
Data indicate that F-box and leucine-rich repeat protein 5 (FBXL5)-Hr (hemerythrin-like domain) undergoes substantive structural changes when iron becomes limiting, accounting for its switch-like behavior.
Detailed molecular and structural characterization of the ligand-responsive hemerythrin domain provides insights into the mechanisms by which FBXL5 serves as a unique mammalian metabolic sensor.
iron homeostasis is regulated by a proteolytic pathway that couples IRP2 (show IREB2 Proteins) degradation to intracellular iron levels through the stability and activity of FBXL5
observations suggest a mechanistic link between iron sensing via the FBXL5 hemerythrin domain, IRP2 (show IREB2 Proteins) regulation, and cellular responses to maintain mammalian iron homeostasis
FBXL5 contributes to regulation of neural stem progenitor cell proliferation during mammalian brain development.
we describe the iron and oxygen sensing mechanisms of the FBXL5 Hr-like domain and its role in mediating ROS (show ROS1 Proteins) biology.
The FBXL5-IRP2 (show IREB2 Proteins) axis is integral to control of iron metabolism in vivo.
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 several tandem leucine-rich repeats. Alternatively spliced transcript variants have been described for this locus.
F-box and leucine-rich repeat protein 5
, F-box/LRR-repeat protein 5
, F-box/LRR-repeat protein 5-like
, F-box protein FBL4/FBL5
, F-box protein FBL5
, p45SKP2-like protein