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首页> 外文期刊>The FEBS journal >The ubiquitin-like protein monoclonal nonspecific suppressor factor o conjugates to endophilin II and regulates phagocytosis
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The ubiquitin-like protein monoclonal nonspecific suppressor factor o conjugates to endophilin II and regulates phagocytosis

机译：泛素样蛋白单克隆非特异性抑制因子o与内吞蛋白II结合并调节吞噬作用

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Monoclonal nonspecific suppressor factor o (MNSFo) is a ubiquitously expressed member of the ubiquitin-like family that has been implicated in various biological functions. Previous studies have demonstrated that MNSFo covalently binds to the intracellular proapoptotic protein Bcl-G in cells of the macrophage cell line Raw264.7, suggesting involvement of this ubiquitin-like protein in apoptosis. In this study, we purified a 62 kDa MNSFo adduct from murine liver lysates by sequential chromatography on DEAE and anti-MNSFo IgG-conjugated Sepharose. MALDI-TOF MS fingerprinting revealed that this MNSFo adduct consists of an 8.5 kDa MNSFo and endophilin II, a member of the endophilin A family. MNSFo may conjugate to endophilin II with a linkage between the C-terminal Gly74 and Lys294. We confirmed this result by immunoprecipitation/western blot studies. Endophilin II was ubiquitously expressed in various tissues, although a truncated form was observed in liver. The 62 kDa MNSFo-endophilin II was specifically expressed in liver and macrophages. Small interfering RNA-mediated knockdown of endophilin II and/or MNSFo promoted phagocytosis of zymosan in Raw264.7 cells. Conversely, cotransfection of endophilin II and MNSFo cDNAs inhibited the phagocytosis of zymosan. Such inhibition was not observed in cells expressing a mutant of endophilin II in which Lys294 was replaced by arginine. These results suggest that the post-translational modification of endophilin II by MNSFo might be implicated in phagocytosis by macrophages. Structured digital abstract MINT-7261558, MINT-7261537, MINT-7261546: MNSF beta (uniprotkb: P35545) physically interacts ( MI:0915) with Endophilin-2 (uniprotkb: Q62419) by anti bait coimmunoprecipitation ( MI:0006)
机译：单克隆非特异性抑制因子o（MNSFo）是遍在蛋白样家族中一个普遍表达的成员，与多种生物学功能有关。先前的研究表明，MNSFo与巨噬细胞系Raw264.7的细胞内细胞凋亡蛋白Bcl-G共价结合，表明该泛素样蛋白参与凋亡。在这项研究中，我们通过在DEAE和抗MNSFo IgG偶联的Sepharose上进行顺序色谱从鼠肝裂解物中纯化了62 kDa MNSFo加合物。 MALDI-TOF MS指纹图谱显示，该MNSFo加合物由8.5 kDa MNSFo和内啡肽II（内啡肽A家族的成员）组成。 MNSF 0可以通过C末端Gly 74和Lys 294之间的连接缀合至内吞蛋白II。我们通过免疫沉淀/蛋白质印迹研究证实了这一结果。尽管在肝脏中观察到了截短形式，但内皮糖蛋白II在各种组织中普遍表达。 62 kDa MNSFo-endophilin II在肝脏和巨噬细胞中特异性表达。 RNA介导的内吞蛋白II和/或MNSFo的小干扰可促进Raw264.7细胞中酵母聚糖的吞噬作用。相反，内吞蛋白II和MNSFo cDNA的共转染可抑制酵母聚糖的吞噬作用。在表达内啡肽II突变体的细胞中未观察到这种抑制，其中Lys294被精氨酸替代。这些结果表明，MNSFo对内吞蛋白II的翻译后修饰可能与巨噬细胞的吞噬作用有关。结构化数字摘要MINT-7261558，MINT-7261537，MINT-7261546：MNSF beta（uniprotkb：P35545）通过抗诱饵免疫共沉淀（MI：0006）与Endophilin-2（uniprotkb：Q62419）物理相互作用（MI：0915）

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