Novel Phosphorylation(新型磷酸化)研究综述
Novel Phosphorylation 新型磷酸化 - VEGFR2 carries out the novel phosphorylation of Y135 within the DRY microswitch of CXCR4, sequentially activating Gαiβγ, AC7 and PKA, which phosphorylates S988 on the integrin. [1] The data demonstrate a novel phosphorylation-dependent mechanism to regulate Gld2 activity, revealing tumour suppressor miRNAs as a previously unknown target of Akt1-dependent signalling. [2] Disruption of this function by disease mutations suggests a novel phosphorylation-independent loss of function mechanism that may synergize with other neurotoxic effects caused by LRRK2 mutations. [3] Preliminary findings show that our hit compound inhibits CDK5 with simultaneous elevation of novel phosphorylation on pS65-PRKAG2 embarking catalytic activation of AMPK kinase. [4] In some cases, novel phosphorylation-dependent regulatory paradigms for cell division, gene transcription, and protein translation have been identified suggesting that a wide scope of prokaryotic physiology remains to be characterized. [5]VEGFR2 在 CXCR4 的 DRY 微开关内对 Y135 进行新的磷酸化，依次激活 Gαiβγ、AC7 和 PKA，它们使整合素上的 S988 磷酸化。 [1] 数据证明了一种新的磷酸化依赖性机制来调节 Gld2 活性，揭示了肿瘤抑制 miRNA 作为 Akt1 依赖性信号传导的先前未知靶标。 [2] 疾病突变对该功能的破坏表明一种新的不依赖磷酸化的功能丧失机制，该机制可能与 LRRK2 突变引起的其他神经毒性作用协同作用。 [3] 初步研究结果表明，我们的命中化合物抑制 CDK5，同时提高 pS65-PRKAG2 上的新磷酸化，从而启动 AMPK 激酶的催化活化。 [4] 在某些情况下，已经确定了用于细胞分裂、基因转录和蛋白质翻译的新型磷酸化依赖性调节范式，这表明仍有广泛的原核生理学特征有待表征。 [5]
novel phosphorylation site 新型磷酸化位点
Mass spectrometric analysis of immunoprecipitated Runx2 protein from HEK293 cells overexpressing MST2 and SAV1 revealed two novel phosphorylation sites at Ser-339 and Ser-370 residues of mouse Runx2 protein. [1] We previously identified a novel phosphorylation site in JFH-1 NS5A: S146. [2] Novel phosphorylation sites were found on IAV-encoded proteins, and the functional analysis of selected phosphorylation sites showed that they either support (NA Ser178) or inhibit (PB1 Thr223) virus propagation. [3] We show that both MCPH1 isoforms are phosphorylated in a cyclin‐dependent kinase‐1–dependent manner in mitosis and identify several novel phosphorylation sites. [4] Here we reveal a novel phosphorylation site of SET isoform 1, and we have determined its biological significance in tumorigenesis. [5] Here, we performed CTCF mass spectrometry, identified a novel phosphorylation site at Serine 224 (Ser224-P), and demonstrate that phosphorylation is carried out by Polo-like kinase 1 (PLK1). [6] Phosphoproteomics and high throughput screening identified novel phosphorylation sites downstream of Cdk5. [7] For functional verification of novel phosphorylation sites, the authors use a binding assay, combining CENP-F containing a phosphomimetic mutation and karyopherin α, a nuclear transport receptor, thus providing cross-validation. [8] CONCLUSION We identified a novel phosphorylation site of DJ-1. [9] Phosphoproteomics revealed four novel phosphorylation sites on the third intracellular loop of the 5-HT1B receptor, and mutations of serine-256 and serine-291 to alanine led to reduced levels of ERK1/2 phosphorylation following receptor activation. [10] We demonstrate that HSD3B2 is phosphorylated at Ser95 or 96 and identify a novel phosphorylation site, Ser489, in CYP21A2, suggesting that steroidogenic enzymes are regulated by phosphorylation. [11] We determined the phosphorylation pattern of MST1 using a phosphoproteomic approach and identified two amino acid residues phosphorylated in an ERK-dependent manner after GDC-0941 treatment together with a novel phosphorylation site at S21 residue, which was extensively phosphorylated in an ERK-independent manner during PI3K signaling blockade. [12] Here, we identified tyrosine 78 residue (Y78) of NP as a novel phosphorylation site by mass spectrometry. [13]对来自过表达 MST2 和 SAV1 的 HEK293 细胞的免疫沉淀 Runx2 蛋白的质谱分析揭示了小鼠 Runx2 蛋白的 Ser-339 和 Ser-370 残基处的两个新磷酸化位点。 [1] 我们之前在 JFH-1 NS5A：S146 中发现了一个新的磷酸化位点。 [2] 在 IAV 编码的蛋白质上发现了新的磷酸化位点，对选定磷酸化位点的功能分析表明它们要么支持 (NA Ser178) 要么抑制 (PB1 Thr223) 病毒传播。 [3] 我们表明，两种 MCPH1 亚型在有丝分裂中都以依赖于细胞周期蛋白的激酶 1 的方式被磷酸化，并确定了几个新的磷酸化位点。 [4] 在这里，我们揭示了 SET 亚型 1 的一个新的磷酸化位点，我们已经确定了它在肿瘤发生中的生物学意义。 [5] 在这里，我们进行了 CTCF 质谱分析，在丝氨酸 224 (Ser224-P) 处鉴定了一个新的磷酸化位点，并证明磷酸化是由 Polo 样激酶 1 (PLK1) 进行的。 [6] 磷酸蛋白质组学和高通量筛选确定了 Cdk5 下游的新磷酸化位点。 [7] 对于新磷酸化位点的功能验证，作者使用结合测定法，将含有拟磷突变的 CENP-F 和核转运蛋白 α（一种核转运受体）结合起来，从而提供交叉验证。 [8] 结论 我们确定了一个新的 DJ-1 磷酸化位点。 [9] 磷酸蛋白质组学揭示了 5-HT1B 受体第三个细胞内环上的四个新磷酸化位点，丝氨酸 256 和丝氨酸 291 突变为丙氨酸导致受体激活后 ERK1/2 磷酸化水平降低。 [10] 我们证明 HSD3B2 在 Ser95 或 96 处被磷酸化，并在 CYP21A2 中鉴定出一个新的磷酸化位点 Ser489，这表明类固醇生成酶受磷酸化的调节。 [11] 我们使用磷酸蛋白质组学方法确定了 MST1 的磷酸化模式，并在 GDC-0941 处理后鉴定了两个以 ERK 依赖性方式磷酸化的氨基酸残基，以及 S21 残基处的新磷酸化位点，在 S21 残基处以不依赖 ERK 的方式广泛磷酸化。 PI3K 信号传导阻滞。 [12] 在这里，我们通过质谱鉴定了 NP 的酪氨酸 78 残基 (Y78) 作为新的磷酸化位点。 [13]