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Description
Purified anti-FBXL5. In metazoans, iron homeostasis is mediated at the systemic and cellular levels by the RNA-binding iron regulatory proteins IRP1 and IRP2.Under conditions where cellular iron is limiting, IRP1 and IRP2 stabilize the mRNA of genes involved in iron acquisition and mobilization and translationally repress genes involved in iron storage and export.? Under iron replete conditions, both IRPs are inactivated: IRP1 acquires an Fe-S cluster that inhibits RNA-binding activity, while IRP2 is targeted for proteasomal-mediated degradation by the E3 ubiquitin ligase FBXL5. Under iron-replete conditions Fe-S cluster biogenesis is disrupted, FBXL5 will also target IRP1 for degradation.FBXL5, or F-box and leucine-rich repeat protein 5 (FBXL5), is the E3 ubiquitin ligase component of the SCFFBXL5 complex. The complex contains SKP1, Cullin-1, RBX1, and FBXL5. When cytosolic iron is replete, FBXL5 recruits IRP2 to the SCF complex and promotes its ubiquitination and subsequent degradation. FBXL5 contains a hemerythrin-like domain that senses oxygen and iron availability. This sensing mechanism is linked to the stability of the FBXL5 protein itself: when cytosolic iron is available, iron binds to the hemerythrin domain and promotes the stability of the FBXL5 protein. When iron is deficient, the FBXL5 protein lacks the iron ligand, resulting in its degradation and activation of the IRP-mediated iron starvation response.Studies have also shown that FBXL5 can ubiquitinate and target the SNAIL1 transcription factor and disruption of this process promotes epithelialto mesenchymal transition.?
Immunogen
Recombinant human FBXL5
Other Names
F-box/LRR-repeat protein 5, F-box and leucine-rich repeat protein 5, F-box protein FBL4/FBL5, p45SKP2-like protein, FBL4, FBL5, FLR1