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- The FBXL family of F-box proteins: variations on a theme
The FBXL family of FBPs is composed of 21 members (Fbxl1–Fbxl8, Fbxl10 –Fbxl22), each characterized by their leucine-rich repeat (LRR) domains An additional potential member is leu-cine-rich repeat-containing protein 29 (LRC29), posited to be Fbxl9
- FBXL6 degrades phosphorylated p53 to promote tumor growth
Mechanistically, FBXL6 targets phospho-p53 (S315) to mediate its polyubiquitination and proteasomal degradation, thereby inhibiting p53 signaling FBXL6 depletion inhibits proliferation of p53
- The F-box protein FBXL-5 governs vitellogenesis and lipid . . .
We identified the Caenorhabditis elegans F-box protein FBXL-5 as a negative regulator of maternal provisioning of vitellogenin lipoproteins, which mediate the transfer of intestinal lipids to the germline
- Fâ box protein lt;fc gt;FBXL lt; fc gt;2 inhibits gastric cancer . . .
F-box LRR-repeat protein 2 (FBXL2), a component of Skp-Cullin-F box (SCF) ubiquitin E3 ligase, has been shown to inhibit tumorigenesis by target-ing and ubiquitinating several oncoproteins However, its role in gastric can-cer remains poorly understood
- The Role of FBXL Subfamily of F-box Proteins in Tumorigenesis
In this chapter, we primarily focus on summarizing the recent genetic, pathological as well as the biochemical evidence pinpointing a possible tumor sup-pressor or oncogenic role for each of the FBXL subfamily member proteins
- The E3 ubiquitin ligase FBXL6 controls the quality of newly . . .
Here, we show that the E3 ubiquitin ligase F box leucine-rich-repeat pro-tein 6 (FBXL6) regulates the quality of cytosolically translated mitochondrial proteins Indeed, we found that FBXL6 substrates are newly synthesized mitochondrial ribosomal proteins
- Functional characterization of FBXL7 as a novel player in . . .
F-box and leucine-rich repeat protein 7 (FBXL7), an F-box protein responsible for substrate recognition by the SKP1-Cullin-1-F-box (SCF) ubiquitin ligases, plays an emerging role in the
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