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    FBXL5 F-box and leucine rich repeat protein 5 [ Homo sapiens (human) ]

    Gene ID: 26234, updated on 27-Nov-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    FBXL5 promotes lipid accumulation in alcoholic fatty liver disease by promoting the ubiquitination and degradation of TFEB.

    FBXL5 promotes lipid accumulation in alcoholic fatty liver disease by promoting the ubiquitination and degradation of TFEB.
    Zhang S, Ji B, Li J, Ji W, Yang C, Yang L.

    11/8/2023
    Loss of F-Box and Leucine Rich Repeat Protein 5 (FBXL5) Expression Is Associated With Poor Survival in Patients With Hepatocellular Carcinoma After Curative Resection: A Two-institute Study.

    Loss of F-Box and Leucine Rich Repeat Protein 5 (FBXL5) Expression Is Associated With Poor Survival in Patients With Hepatocellular Carcinoma After Curative Resection: A Two-institute Study.
    Cho YA, Kim SE, Park CK, Koh HH, Park CK, Ha SY., Free PMC Article

    04/26/2023
    Ferroportin and FBXL5 as Prognostic Markers in Advanced Stage Clear Cell Renal Cell Carcinoma.

    Ferroportin and FBXL5 as Prognostic Markers in Advanced Stage Clear Cell Renal Cell Carcinoma.
    Park CK, Heo J, Ham WS, Choi YD, Shin SJ, Cho NH., Free PMC Article

    02/12/2022
    This study has identified an iron-sulfur cluster within FBXL5, which promotes IRP2 polyubiquitination and degradation in response to both iron and oxygen concentrations.

    FBXL5 Regulates IRP2 Stability in Iron Homeostasis via an Oxygen-Responsive [2Fe2S] Cluster.
    Wang H, Shi H, Rajan M, Canarie ER, Hong S, Simoneschi D, Pagano M, Bush MF, Stoll S, Leibold EA, Zheng N., Free PMC Article

    07/25/2020
    Dysregulation of FBXL5-mediated cellular iron homeostasis was found to be associated with poor prognosis in human hepatocellular carcinoma, suggesting that FBXL5 plays a key role in defense against hepatocarcinogenesis.

    Disruption of FBXL5-mediated cellular iron homeostasis promotes liver carcinogenesis.
    Muto Y, Moroishi T, Ichihara K, Nishiyama M, Shimizu H, Eguchi H, Moriya K, Koike K, Mimori K, Mori M, Katayama Y, Nakayama KI., Free PMC Article

    05/9/2020
    We demonstrate that the CIA-targeting complex promotes the ability of FBXL5 to degrade iron regulatory proteins. In addition, the FBXL5-CIA-targeting complex interaction is regulated by oxygen (O2) tension displaying a robust association in 21% O2 that is severely diminished in 1% O2 and contributes to O2-dependent regulation of IRP degradation

    An Oxygen-Dependent Interaction between FBXL5 and the CIA-Targeting Complex Regulates Iron Homeostasis.
    Mayank AK, Pandey V, Vashisht AA, Barshop WD, Rayatpisheh S, Sharma T, Haque T, Powers DN, Wohlschlegel JA., Free PMC Article

    01/25/2020
    MiR-1306-3p directly targets FBXL5 and modulates FBXL5-meadiated snail protein stability in hepatocellular carcinoma.

    miR-1306-3p targets FBXL5 to promote metastasis of hepatocellular carcinoma through suppressing snail degradation.
    He ZJ, Li W, Chen H, Wen J, Gao YF, Liu YJ.

    06/1/2019
    this study demonstrated that FBXL5 functioned as an oncogene in the progression of colon cancer through regulating PTEN/PI3K/AKT signaling

    F-box and leucine-rich repeat protein 5 promotes colon cancer progression by modulating PTEN/PI3K/AKT signaling pathway.
    Yao H, Su S, Xia D, Wang M, Li Z, Chen W, Ren L, Xu L.

    01/5/2019
    Transcriptomic analysis shows downregulation of FBXL5 expression in HSCs of patients with myelodysplastic syndrome.

    Essential role of FBXL5-mediated cellular iron homeostasis in maintenance of hematopoietic stem cells.
    Muto Y, Nishiyama M, Nita A, Moroishi T, Nakayama KI., Free PMC Article

    12/29/2018
    regulatory circuit involving FBXL5 and CIA acts through both IRPs to control iron metabolism and promote optimal cell growth

    A synergistic role of IRP1 and FBXL5 proteins in coordinating iron metabolism during cell proliferation.
    Johnson NB, Deck KM, Nizzi CP, Eisenstein RS., Free PMC Article

    10/14/2017
    analysis of the redox sensing mechanism by which FBXL5 can serve as an iron metabolism regulator within mammalian cells

    Redox sensing molecular mechanism of an iron metabolism regulatory protein FBXL5.
    Wei Y, Yuan H, Xu P, Tan X.

    05/20/2017
    FBXL5 regulates cortactin through induction of its ubiquitylation, and FBXL5 similarly regulates Snail1.

    FBXL5 inhibits metastasis of gastric cancer through suppressing Snail1.
    Wu W, Ding H, Cao J, Zhang W.

    01/2/2016
    FBXL5-mediated degradation of CITED2 leads to the activation of HIF-1alpha.

    FBXL5 modulates HIF-1α transcriptional activity by degradation of CITED2.
    Machado-Oliveira G, Guerreiro E, Matias AC, Facucho-Oliveira J, Pacheco-Leyva I, Bragança J.

    08/15/2015
    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

    HERC2 targets the iron regulator FBXL5 for degradation and modulates iron metabolism.
    Moroishi T, Yamauchi T, Nishiyama M, Nakayama KI., Free PMC Article

    10/11/2014
    F-box and leucine-rich repeat protein 5 (FBXL5) is required for maintenance of cellular and systemic iron homeostasis

    F-box and leucine-rich repeat protein 5 (FBXL5) is required for maintenance of cellular and systemic iron homeostasis.
    Ruiz JC, Walker SD, Anderson SA, Eisenstein RS, Bruick RK., Free PMC Article

    03/2/2013
    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.

    Hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5) communicates cellular iron and oxygen availability by distinct mechanisms.
    Chollangi S, Thompson JW, Ruiz JC, Gardner KH, Bruick RK., Free PMC Article

    10/13/2012
    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.

    Structural and molecular characterization of iron-sensing hemerythrin-like domain within F-box and leucine-rich repeat protein 5 (FBXL5).
    Thompson JW, Salahudeen AA, Chollangi S, Ruiz JC, Brautigam CA, Makris TM, Lipscomb JD, Tomchick DR, Bruick RK., Free PMC Article

    04/28/2012
    observations suggest a mechanistic link between iron sensing via the FBXL5 hemerythrin domain, IRP2 regulation, and cellular responses to maintain mammalian iron homeostasis

    An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis.
    Salahudeen AA, Thompson JW, Ruiz JC, Ma HW, Kinch LN, Li Q, Grishin NV, Bruick RK., Free PMC Article

    01/21/2010
    iron homeostasis is regulated by a proteolytic pathway that couples IRP2 degradation to intracellular iron levels through the stability and activity of FBXL5

    Control of iron homeostasis by an iron-regulated ubiquitin ligase.
    Vashisht AA, Zumbrennen KB, Huang X, Powers DN, Durazo A, Sun D, Bhaskaran N, Persson A, Uhlen M, Sangfelt O, Spruck C, Leibold EA, Wohlschlegel JA., Free PMC Article

    01/21/2010
    Our findings provide a potential mechanism by which p150(Glued) protein function is regulated by SCFs.

    FBXL5 interacts with p150Glued and regulates its ubiquitination.
    Zhang N, Liu J, Ding X, Aikhionbare F, Jin C, Yao X.

    01/21/2010
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