The F‐box protein <scp>FBXL</scp>18 promotes glioma progression by promoting K63‐linked ubiquitination of Akt

Zhang, Jindong; Yang, Zhifen; Ou, Jiayu; Xia, Xiaojun; Zhi, Feng; Cui, Jun

doi:10.1002/1873-3468.12521

Cited by 24 publications

(22 citation statements)

References 30 publications

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“…We observed that EGF reproducibly increased Cul1 assembly of not only Skp2, but also βTrCP1 and FBXL18 by >2-fold (Fig 6A; Table S2E), suggesting roles for the latter two proteins in the EGF response. Indeed, FBXL18 has been linked to EGF signaling (Zhang et al, 2017). Western blot analysis revealed that DKO cells had a higher resting level of p-AKT and Skp2•Cul1 complex, but that the EGF-induced assembly of Skp2 with Cul1 was dependent on Cand1/2 and Nedd8 conjugation (Fig.…”

Section: Resultsmentioning

confidence: 99%

Composition and Regulation of the Cellular Repertoire of SCF Ubiquitin Ligases

Reitsma

Liu

Reichermeier

et al. 2017

Cell

123

129

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Summary SCF (Skp1-Cullin-F-box) ubiquitin ligases comprise several dozen modular enzymes that have diverse roles in biological regulation. SCF enzymes share a common catalytic core containing Cul1•Rbx1, which is directed towards different substrates by a variable substrate receptor (SR) module comprising one of 69 F-box proteins bound to Skp1. Despite the broad cellular impact of SCF enzymes, important questions remain about the architecture and regulation of the SCF repertoire, including whether SRs compete for Cul1, and if so, how this competition is managed. Here, we devise methods that preserve the in vivo assemblages of SCF complexes, and apply quantitative mass spectrometry to perform a census of these complexes (the ‘SCFome’) in various states. We show that Nedd8 conjugation and the SR exchange factor Cand1 have a profound effect on shaping the SCFome. Together, these factors enable rapid remodeling of SCF complexes to promote biased assembly of SR modules bound to substrate.

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Section: Resultsmentioning

confidence: 99%

Composition and Regulation of the Cellular Repertoire of SCF Ubiquitin Ligases

Reitsma

Liu

Reichermeier

et al. 2017

Cell

123

129

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“…Abnormal expression or dysfunction of several F-box proteins results in aberrant ubiquitination, inducing the development and progression of malignancies, including hematopoietic malignancies. Some F-box family members contribute to tumorigenesis and tumor development 13 – 15 . Fbxw7 controls leukemia-initiating cells in chronic myelogenous leukemia and chronic myeloid leukemia (CML) by regulating c-Myc ubiquitination 16 – 18 .…”

Section: Introductionmentioning

confidence: 99%

Fbxw11 promotes the proliferation of lymphocytic leukemia cells through the concomitant activation of NF-κB and β-catenin/TCF signaling pathways

et al. 2018

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The ubiquitin–proteasome system (UPS) participates in both physiological and pathological processes through the posttranslational regulation of intracellular signal transduction pathways. F-box and WD-40 domain protein 11 (Fbxw11) is a component of the SCF (Skp1–Cul1–F-box) E3 ubiquitin ligase complex. Fbxw11 regulates various signal transduction pathways, and it may have pathological roles in tumorigenesis. However, the role of Fbxw11 in the development of leukemia and the underlying mechanisms remain largely unknown. In this study, Fbxw11 expression was aberrantly upregulated in patients with lymphocytic leukemia. Its expression was dramatically decreased in patients who achieved complete remission (CR) after chemotherapy. The high level of Fbxw11 expression in L1210 lymphocytic leukemia cells stimulated cell proliferation in vitro and tumor formation in vivo. The effects were mediated by the stimulation of cell cycle progression rather than the induction of apoptosis. Furthermore, a bioinformatics analysis suggested concomitant activation of the NF-κB and β-catenin/TCF signaling pathways, which were confirmed by reporter gene assays. Moreover, blocking experiments suggested the involvement of both pathways in the growth-promoting effects of Fbxw11. Our results reveal the role of Fbxw11 in lymphocytic leukemia cells and imply that Fbxw11 may serve as a potential molecular target for the treatment of lymphocytic leukemia.

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“…F-box proteins promote the ubiquitin-proteasome system ( Halbach et al., 2015 ; Murdoch et al., 2016 ; Sandoval et al., 2015 ; Teixeira et al., 2013 ; Trausch-Azar et al., 2015 ; Yalla et al., 2018 ; Zheng et al., 2016 ) and interact with cell cycle progression ( Randle and Laman, 2016 ; Zhang et al., 2017 ). One F-box protein, FBXW2, has been identified as a housekeeping gene ( Almeida et al., 2014 ), but the functions of FBXW2 are largely unknown.…”

Section: Introductionmentioning

confidence: 99%

FBXW2 localizes with osteocalcin in bovine periosteum on culture dishes as visualized by double immunostaining

Akiyama

2018

Heliyon

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Osteocalcin (OC) is a well-known protein related to bone, however, the role of F-box and WD-40 domain-containing protein 2 (FBXW2) in bone remains unclear. In 2016, the presence of FBXW2 in bovine periosteum was reported. In this study, double immunostaining was used to investigate the relationship between OC and FBXW2. FBXW2 showed tubular structures, and OC showed a similar localization pattern as FBXW2. Double immunostaining findings suggested that FBXW2 tubes were coated with OC. To the author's knowledge, this is the first study to reveal the interaction between OC and FBXW2.

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The F‐box protein FBXL18 promotes glioma progression by promoting K63‐linked ubiquitination of Akt

Cited by 24 publications

References 30 publications

Composition and Regulation of the Cellular Repertoire of SCF Ubiquitin Ligases

Composition and Regulation of the Cellular Repertoire of SCF Ubiquitin Ligases

Fbxw11 promotes the proliferation of lymphocytic leukemia cells through the concomitant activation of NF-κB and β-catenin/TCF signaling pathways

FBXW2 localizes with osteocalcin in bovine periosteum on culture dishes as visualized by double immunostaining

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