Ask about this productRelated genes to: FEM1B antibody
- Gene:
- FEM1B NIH gene
- Name:
- fem-1 homolog B
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 15q23
- Locus Type:
- gene with protein product
- Date approved:
- 1999-05-25
- Date modifiied:
- 2016-10-05
Related products to: FEM1B antibody
Related articles to: FEM1B antibody
- Lung cancers frequently increase iron demand to sustain growth, which makes them vulnerable to ferroptosis. While Cullin 2-RING ubiquitin ligases (CRL2s) are critical regulators of stress responses and redox balance, their role in ferroptosis mechanisms remains largely unknown. Here, we identify the E3 ligase CRL2 as a key regulator of the ferroptotic response. CRL2 recruits BTB and CNC homolog 1 (BACH1), a transcriptional regulator of ferroptosis, for degradation by recognizing a degron that is directly formed by the redox-sensing molecule heme. By degrading BACH1 in response to heme, CRL2 acts as a switch that dynamically modulates the transcriptional activation of ferroptosis-protective genes, particularly solute carrier family 7 member 11 (SLC7A11). Loss of CRL2 stabilizes BACH1 and suppresses SLC7A11, thereby sensitizing lung tumor cells to ferroptosis inducers in vitro and in preclinical models. Our findings identify CRL2 as a target to increase the efficacy of ferroptosis inducers in lung cancer treatment and define a broader principle whereby endogenous metabolites regulate protein degradation by enabling substrate-E3 ligase interactions. - Source: PubMed
Publication date: 2026/05/04
Ahmed BashirSalaun DanieleJordan Jack BDaulat AvaisPastorello ChiaraBrito TarcísioYang YuyingJosselin EmmanuelleByrne DeborahBetzi StephanePelletier AmandineVernerey JulienFerreira LoreneCastellano RemyAudebert StephaneCamoin LucPane AttilioBechara CherineBorg Jean-PaulModesti MauroLignitto Luca - The embryonic stages of Eriocheir sinensis are critical for establishing early sex-differentiation signals, yet the molecular mechanisms remain unclear, partly due to the long-standing lack of effective techniques for sex identification in embryos. In this study, sex was distinguished using a sex-specific molecular marker available exclusively in our research group. Transcriptome sequencing combined with weighted gene co-expression network analysis (WGCNA) was then employed to compare sex-biased gene expression across three embryonic stages (blastula, gastrula, and egg-nauplius). Results showed a "development-dominated, sex-emerging" transcriptional pattern. WGCNA identified 19 co-expression modules in which the gene expression was mainly different among developmental stages. Only a clear sex bias was showed at the blastula stage with green and light-yellow modules. Combined with differentially expressed genes (DEGs), the germline and reproduction related genes (VASA, WNT7, FTZ-F1, and GATA4) were upregulated at the male blastula. Notably, the marked sex regulators (Sxl, tra-2c, fem-1b, runt1a, FoxL2, and Sox-14) showed stage-dependent expression and peaked at the gastrula stage, as supported by both DEG analysis and Mfuzz trend clustering. This gastrula-peaked pattern was accompanied by enrichment of spliceosome and nucleocytoplasmic transport pathways in both sexes. It is suggested that sex differences during embryo genesis may partly be shaped at the RNA/splicing level. These findings reveal the connection between developmental and sex-regulatory programs in E. sinensis embryo stages, providing new molecular insights into crustacean sex differentiation. - Source: PubMed
Publication date: 2026/02/10
Liu YourongShao ShuchengYang YananNi MengqiXue XinruZheng JinbinZhang YiLi BenzhenCui Zhaoxia - Targeted protein degradation using PROTACs (PROteolysis TArgeting Chimeras) has emerged as a transformative therapeutic strategy, largely relying on a small number of E3 ubiquitin ligases such as CRBN and VHL. However, resistance, toxicity, and poor oral bioavailability limit the utility of PROTACs and highlight the need to expand the E3 ligase toolbox. Fem-1 homolog B (FEM1B) is a lesser-known E3 ligase that offers a promising alternative due to its broad expression and ability to recognize diverse degron motifs. Here, we describe the development of a stable construct of FEM1B, the results of a protein-observed NMR-based fragment screen using this construct, and the X-ray structures of some of the fragment hits when bound to the protein. From these results, new PROTACs utilizing FEM1B as the E3 ligase may be discovered, providing an alternative E3 ligase for targeted protein degradation. - Source: PubMed
Katinas Jade MAmporndanai KangsaTaylor Ashley JRose Kristie LGareiss Peter CCrespo Roberto APhan JasonWaterson Alex GFesik Stephen W - FEM1B is recognized for its significant pro-apoptotic function in colorectal cancer; however, its influence and mechanisms regarding apoptosis in immune cells remain inadequately elucidated. In this study, we demonstrated that FEM1B enhances TRAIL-induced apoptosis in Molt-4, Jurkat, THP-1, and U937 cell lines. Notably, the knockdown of FEM1B in transfected cells resulted in a reversal of the observed increase in cell apoptosis. Our findings indicate that FEM1B activates caspase-3 and caspase-8, but not caspase-9, in response to TRAIL stimulation, suggesting its involvement in the extrinsic caspase-dependent apoptotic pathway. Furthermore, we found that FEM1B interacted with TRAF2 and downregulates its expression in Molt-4 and Jurkat cells, thereby diminishing TRAF2's inhibitory effect on caspase-8. In THP-1 and U937 cells, FEM1B was found to upregulate TRAIL-R2, thereby promoting TRAIL-induced apoptosis. Knockout studies in murine models further corroborated that FEM1B facilitates TRAIL-induced apoptosis. These results demonstrate that FEM1B enhances TRAIL-induced apoptosis in T lymphocytes and monocytes through a caspase-dependent mechanism involving TRAF2 or TRAIL receptors. - Source: PubMed
Publication date: 2025/05/20
Yang ChenboYu WenhuiDang CuiZhang JingjingLu JiahanXue Jing - Mitochondrial homeostasis is maintained through complex regulatory mechanisms, including the balance of mitochondrial dynamics involving fusion and fission processes. A central player in this regulation is the ubiquitin-proteasome system (UPS), which controls the degradation of pivotal mitochondrial proteins. In this study, we identified cullin-RING E3 ligase 2 (CRL2) and its substrate receptor, FEM1B, as critical regulators of mitochondrial dynamics. Through proteomic analysis, we demonstrate here that FEM1B controls the turnover of PLD6, a key regulator of mitochondrial dynamics. Using structural and biochemical approaches, we show that FEM1B physically interacts with PLD6 and that this interaction is facilitated by the direct association of FEM1B with the mitochondrial import receptor TOM20. Ablation of FEM1B or disruption of the FEM1B-TOM20 interaction impairs PLD6 degradation and induces mitochondrial defects, phenocopying PLD6 overexpression. These findings underscore the importance of FEM1B in maintaining mitochondrial morphology and provide further mechanistic insights into how the UPS regulates mitochondrial homeostasis. - Source: PubMed
Publication date: 2025/04/22
Raiff AnatZhao ShidongBekturova AizatZenge ColinMazor ShirChen XinyanRu WenwenMakaros YaaraAst TslilOrdureau AlbanXu ChaoKoren Itay