Ask about this productRelated genes to: MLN64 antibody
- Gene:
- STARD3 NIH gene
- Name:
- StAR related lipid transfer domain containing 3
- Previous symbol:
- -
- Synonyms:
- es64, MLN64
- Chromosome:
- 17q11-q12
- Locus Type:
- gene with protein product
- Date approved:
- 2002-10-08
- Date modifiied:
- 2015-11-20
Related products to: MLN64 antibody
Related articles to: MLN64 antibody
- Carotenoids are hydrophobic pigments that confer coloration in marine invertebrates, but the underlying mechanisms often remain underexplored. Here, we demonstrate that the recently discovered STARD3-like protein from the selectively bred, commercially valuable golden noble scallop Mimachlamys nobilis (MnSTARD3L) contains a bona fide water-soluble carotenoid-binding domain. Using in vitro reconstitution and expression in carotenoid-synthesizing Escherichia coli, we show that the ~25-kDa START domain of MnSTARD3L binds multiple xanthophylls, including astaxanthin, zeaxanthin and canthaxanthin, inducing ~20-nm bathochromic shifts typical of functional carotenoid-protein complexes. Remarkably, MnSTARD3L preferentially accumulates the rare oxidation products, aporhodoxanthinone and trioxoeschscholtzxanthone, even in vast zeaxanthin excess. Such selectivity was rationalized by structural modeling using modern deep learning algorithms. MnSTARD3L displays no intrinsic carotenoid oxidase activity but functions as a carotenoid transfer protein, selectively donating zeaxanthin to the silkworm homolog BmCBP and aporhodoxanthinone to the unrelated cyanobacterial protein AnaCTDH. Thus, despite its acidic isoelectric point and low sequence identity with alkaline BmCBP, MnSTARD3L is also a functional carotenoid transporter, yet with distinct ligand preferences, likely dictated by peculiarities of its lipid-binding cavity and Ω1 loop. Our findings expand the repertoire of known carotenoproteins and provide mechanistic insights into how homologous protein scaffolds adapt to perform carotenoid binding and transfer functions. - Source: PubMed
Publication date: 2026/04/01
Egorkin Nikita ASlonimskiy Yury BDominnik Eva ELi YuGe BaoshengSluchanko Nikolai N - Membrane contact sites (MCS) are dynamic regions where the membranes of two organelles come into close apposition. MCSs play many roles in cellular homeostasis by facilitating inter-organelle lipid exchange and organelle positioning. The late endosome/lysosome (LE/Lys) cholesterol transfer protein STARD3 forms reversible contacts between LE/Lys and the endoplasmic reticulum (ER). This tether protein contains a Phospho-FFAT motif (two phenylalanines in an acidic tract) whose interaction with ER-resident VAPs (vesicle-associated membrane protein-associated proteins) is phosphorylation-dependent. In this study, we identify GSK3α and GSK3β as the kinases responsible for phosphorylating serine 209 within the Phospho-FFAT motif of STARD3. This phosphorylation event is both necessary and sufficient to activate STARD3's tethering activity, thereby promoting ER-LE/Lys contacts. Furthermore, we show that when ER-LE/Lys tethering is prevented, STARD3 triggers LE/Lys homotypic interactions, revealing an additional function for STARD3 on endosome biology. Our findings establish a direct and critical role for GSK3 in regulating MCS via STARD3 phosphorylation, and expand our understanding of the molecular basis of inter-organelle communication. - Source: PubMed
Publication date: 2026/02/25
Eichler JulieWendling CorinneHuver SophieZouiouich MehdiHanss VictorCardinal AnnaFimbel VictoriaBirck CatherineMcEwen Alastair GKnorr CélineFromental-Ramain CatherineBoutry MaximeChenard Marie-PierreDrin GuillaumeTomasetto CatherineAlpy Fabien - Granulosa cells of the ovary (GOC) served as a core component of the follicular microenvironment, playing a crucial role in regulating steroid hormone synthesis and maintaining pregnancy initiation during key reproductive processes. Arginine (Arg) was a key amino acid in follicular fluid that played a potential role in regulating animal reproduction. However, the mechanism by which it controlled the secretion of steroid hormones by ovarian granulosa cells during the initiation of pregnancy remained unclear. In this study, primary porcine ovarian granulosa cells were used to investigate the effects of arginine on cell proliferation, steroid hormone synthesis, and the underlying molecular mechanisms related to pregnancy maintenance. Results showed that the average arginine concentration in follicles measuring 3-8 mm in diameter was 2.7 mM. Based on these measurements, five arginine supplementation groups were established. Findings indicated that the 4.2 mM arginine group exhibited the highest granulosa cell proliferation efficiency, significantly higher than the control group ( < 0.01). The 4.2 mM arginine group significantly upregulated the expression of genes related to cell proliferation, cell cycle, and apoptosis. Concurrently, the 4.2 mM arginine group upregulated the expression of steroid hormone synthesis-related genes ( < 0.01) and ( < 0.01), thereby promoting estradiol synthesis. Transcriptome sequencing revealed the molecular mechanism by which arginine promoted proliferation and hormone secretion in porcine ovarian granulosa cells. The study found that arginine significantly upregulated the expression of and , key genes in the cholesterol metabolism pathway. This study underscored the pivotal function of arginine in the regulation of reproduction, elucidating its influence on cellular cholesterol metabolism, the promotion of porcine ovarian granulosa cell proliferation, the inhibition of apoptosis, the enhancement of cellular activity, and the facilitation of steroid hormone synthesis through the mediation of and . - Source: PubMed
Publication date: 2026/02/04
Zhang TianruiLu XintanWang XinyiLiu ZebeiShao XuwenHan RuiChe Dongsheng - Bone repair following large defects remains a significant clinical challenge due to limited osteogenic capacity. F-box only protein 6 (FBXO6), an E3 ubiquitin ligase known to promote degradation of downstream proteins, was highly expressed after osteogenic differentiation. Herein, the role of FBXO6 in osteoblastic differentiation and bone remodeling was explored. Rat bone marrow mesenchymal stem cells (BMSCs) were first isolated and characterized. Following 14 days of osteogenic induction, FBXO6 was significantly upregulated (approximately 4-fold increase). BMSCs overexpressing FBXO6 demonstrated enhanced osteogenic potential, evidenced by increased mRNA expression of osteogenic markers (runt-related transcription factor 2, osteocalcin, COL1A1), elevated alkaline phosphatase (ALP) activity, and greater formation of calcium nodules. Conversely, FBXO6-silenced BMSCs exhibited the opposite effects. FBXO6 overexpression activated the Wnt/β-catenin signaling pathway, a known mediator of osteogenic differentiation. This effect was reversed by treatment with the Wnt/β-catenin inhibitor DKK1. Furthermore, β-catenin overexpression rescued the impaired osteogenesis caused by FBXO6 silencing. Label-Free Quantitative Proteomics analysis identified 439 differentially expressed proteins in FBXO6-overexpressing cells (245 upregulated, 194 downregulated). STARD3 N-terminal like protein (STARD3NL) was prioritized for further investigation (log2FC = -0.97, p = 0.02). FBXO6 interacted with STARD3NL and promoted its destabilization. STARD3NL knockdown attenuated the effects of FBXO6 silencing on osteogenesis. In a 3-mm-diameter critical-size femoral defect model, implantation of collagen scaffolds seeded with FBXO6-downregulated BMSCs significantly suppressed osteogenesis. These findings demonstrate that FBXO6-modified BMSC implantation represents a promising therapeutic strategy for bone defect repair. - Source: PubMed
Publication date: 2026/01/01
Yang KerongYue XiWu JinliangChen GuanhaoYang ShuminMa HaojunTan Hongyu - Aldosterone-producing adenomas, a prevalent cause of endocrine hypertension, arise from uncontrolled aldosterone production. NPC1 (NPC intracellular cholesterol transporter 1) is a cholesterol transporter located on the lysosomal limiting membrane. Although cholesterol serves as the primary precursor for aldosterone synthesis, the mechanism governing its supply and metabolism within aldosterone-producing adenomas remains unclear. - Source: PubMed
Publication date: 2025/10/28
Chen JunChen MiaoyunHu JinboWu ZhipengLi HongjiLi WuchaoHe FurongPeng ChuanXu YongHuang WeiGao RufeiLi QifuMa LinqiangYang Shumin