Serine Residues(丝氨酸残基)研究综述
Serine Residues 丝氨酸残基 - Are the environments different between the isosteric serine and cysteine residues? Do some environments promote the formation of cystine S–S bonds? With the increasing availability of structural data for water-insoluble membrane proteins, are there environmental differences for these residues between soluble and membrane proteins? The environments surrounding serine and cysteine residues are dramatically different: serine residues are about 50% solvent exposed, while cysteines are only 10% exposed; the latter are more involved in hydrophobic interactions although there are backbone angle-dependent differences. [1] In human and fish PLK homologs, dephosphorylation of serine residues corresponding to TbPLK Thr125 also reduces kinase activity, demonstrating conservation of this important mechanism for precisely regulating PLK activity during the cell cycle. [2] We propose that context-dependent and mTOR-mediated multisite phosphorylation of serine residues of NBCe1 is likely to be a potent mechanism contributing to the response of astrocytes to acid/base challenges during pathophysiological conditions. [3] Threonine or serine residues at this position in alcohol dehydrogenases are highly conserved and contribute substantially to catalysis. [4] Phosphorylation of the activation loop serine residues (S177, S181) in IKKβ is a key event that drives tumor necrosis factor (TNF) α induced NF-κB mediated gene expression. [5] The members of the Nedd4 family are known to recognize substrates through their multiple WW domains, which recognize PY motifs (PPxY, LPxY) or phospho-threonine or phospho-serine residues. [6] l-Serine residues are site-selectively and residue-specifically adsorbed on the pore surface via multiple hydrogen bonds. [7] We demonstrate that PspA binds to host-derived glyceraldehyde-3-phosphate dehydrogenase (GAPDH) bound to outward-flipped phosphatidylserine residues on dying host cells. [8] Recently, Histone PARylation Factor (HPF1) was shown to be a critical modulator of the activity of PARP1 by facilitating PARylation of histones and redirecting the target amino acid specificity from acidic to serine residues. [9] Mutation of the phosphorylated serine residues 20, 22 and 24 in the cytosol-exposed N-terminus of NRAMP1 alters its membrane distribution. [10] This resource reveals glycosylation occurs exclusively at serine residues and that glycoproteins/glycosylation sites are highly conserved across 294 publicly available B. [11] Here, we report the development of an efficient and modular semisynthetic route to full-length ADP-ribosylated histones H3 and H2B, chemically installed at specific serine residues. [12] Specifically, we identify three serine residues within PARP1 (499, 507, and 519) as key sites whose efficient HPF1-dependent modification counters PARP1 trapping and contributes to inhibitor tolerance. [13] We show that the inositol pyrophosphate 5-IP7 transfers its high-energy beta phosphate moiety to pre-phosphorylated serine residues in the central PEST domain of MYC. [14] showed that the N-terminal region of the yeast Gγ subunit Ste18 contains two serine residues within an intrinsically disordered region that were phosphorylated by different kinases in response to distinct stimuli. [15] The major aggregating protein in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), the RNA-binding protein TDP-43, is hyperphosphorylated in disease on several C-terminal serine residues, which is generally believed to promote TDP-43 aggregation. [16] This parasite breaks the species barrier via hijacking the host's physiological A-like/Tn formation through abundantly expressing serine residues and creating hybrid Alike/Tn structures, which in the human blood group O(H) are attacked by the germline-encoded nonimmune polyreactive immunoglobulin M (IgM), exerting the highly anti-A/B/H-aggressive isoagglutinin activities. [17] Among them, two serine residues at amino acid positions 1332 and 1346 (S1332 and S1346) were certainly phosphorylated in human HeLa cells, but other two serine residues (S1616 and S1691) were not phosphorylated. [18] Resveratrol promotes the binding between LKB1 and Sirt1, which we first reported, and this binding leads to LKB1-mediated phosphorylation of Sirt1 at three different serine residues in the C terminus of Sirt1. [19] Methods Site-directed Mutagenesis was performed to generate a Che-1 mutant (Che-1 3S) lacking three serine residues (Ser 316 , Ser 320 and Ser 321 ) in 308–325 aa region. [20] We show that AMPK mediates phosphorylation of TFEB and TFE3 on three serine residues, leading to TFEB/TFE3 transcriptional activity upon nutrient starvation, FLCN depletion and pharmacological manipulation of mTORC1 or AMPK. [21] We also identified a series of serine residues required for cytokine-dependent transactivation of Nur77. [22] To find functional splice sites in aminoglycoside adenylyltransferase we apply a streamlined strategy looking exclusively at the flexibility of native cysteine and serine residues, which we first validated splitting the enzymes conferring resistance towards ampicillin, kanamycin, chloramphenicol and hygromycin. [23] Three different Pd complexes were incorporated into two different genetically modified enzyme variants, one containing all the natural cysteine residues changed to serine residues, and another variant including an additional Cys mutation directly in the catalytic serine (Ser114Cys). [24] , serine residues intended to receive the D-xylose molecule for initiating HS chains). [25] The use of immunoprecipitation and cell surface biotinylation revealed that DAT is phosphorylated at serine residues, ubiquitinated and released into late endosomes through a PKCβ-dependent mechanism. [26] While Musashi is best characterized as a repressor of target mRNA translation, we have shown that Musashi can activate target mRNA translation in a cell context specific manner via regulatory phosphorylation on two evolutionarily conserved C-terminal serine residues. [27] According to the conserved serine residues at C-terminal, all the ACS genes could be characterized into three groups, which were supported by the exon-intron organizations and conserved motif distributions. [28] The binding of HPF1 on PARP1 controls the grafting of ADP-ribose moieties on serine residues of proteins nearby the DNA lesions, mainly PARP1 and histones. [29] Proteoglycans (PGs) are proteins with glycosaminoglycan (GAG) chains, such as chondroitin sulfate (CS) or heparan sulfate (HS), attached to serine residues. [30] The study has predicted 19 phosphorylation sites on serine residues for protease Carboxypeptidase A1 in S1 strains of S. [31] Alt-RPL36 contains four phosphoserine residues, point mutations of which abolish interaction with TMEM24 and, consequently, alt-RPL36 effects on PI3K signaling and cell size. [32] Phosphorylation of STAT5a serine residues, S726 and S780, may regulate STAT5a in such a way to underlie this duality. [33] The mycomembrane is typified by long-chain mycolic acids that are esterified to various acceptors, including: (1) trehalose, forming trehalose mono- and di-mycolate; (2) arabinogalactan, forming arabinogalactan-linked mycolates; and (3) in some species, protein serine residues, forming O-mycoloylated proteins. [34] The Golgi linking proteins GRASP55 and GRASP65 are PR-ubiquitinated on multiple serine residues, thus preventing their ability to cluster and form oligomeric structures. [35] The serratamolide homologues were comprised of a peptide moiety of two L-serine residues (cyclic or open-ring) linked to two fatty acid chains (lengths of C10, C12, or C12:1). [36] By mass spectrometry, we identified four serine residues within the N-terminus (S26, S29, S541, and S542) constitutively phosphorylated in the mouse ortholog. [37] Previous research on the esterase enzyme mechanisms revealed that the active sites of esterases contain serine residues that catalyze reactions via a nucleophilic attack on the substrates. [38] During the repair of DNA lesions, PARP1 and PARP2 combine with an accessory factor HPF1, which is required for the modification of target proteins on serine residues. [39] Although three conserved serine residues in CRTCs have been implicated in their phosphorylation regulation, how they mediate interactions with 14-3-3 is unclear. [40] Nth1 is known to be phosphorylated by the metabolic kinase PKA on four serine residues and by the cell cycle kinase CDK on one residue. [41] While the unphosphorylated serine residues do not directly interact with ERK2, the phosphorylated Ser-116 engages in strong interactions with arginine residues on FADD DED. [42] PDHA1 contains three serine residues that can be reversibly phosphorylated by a dedicated family of four inhibitory pyruvate dehydrogenase kinases (PDHK1-4) and two reactivating phosphatases (PDP1,2). [43] GIV is rapidly phosphoregulated on key tyrosine and serine residues in human and murine spermatozoa. [44] Phosphorylation at specific serine residues of HSP27, OSR1, and MARCKS, as well as the respective upstream kinases activated by FPR2 stimulation was analysed. [45] Initially it was proposed that Wnts are lipid-modified at their conserved cysteine and serine residues (C77 and S209 in mWnt3a), and mutations in either residue impedes its secretion and activity. [46] We also found that interferon treatment reduces levels of phosphorylation at these serine residues and outline a homeostatic regulatory mechanism in which repression of MX2 by phosphorylation, together with MLCP-mediated dephosphorylation, balances the deleterious effects of MX2 on normal cell function with innate immunity against HIV-1. [47] Importantly, we discovered that circGNG7 could bind to serine residues 78 and 82 of the functional heat shock protein 27 (HSP27), occupying its phosphorylation sites and hindering its phosphorylation, which reduced HSP27-JNK/P38 mitogen-activated protein kinase (MAPK) oncogenic signaling. [48] Phosphorylation at serine residues by CK1 and CK2 modulates its intracellular localization and its sensitivity to kinases or phosphatases. [49] Ae4 sequence analysis showed two potential PKA phosphorylation serine residues located at the intracellular N-terminal domain according to a homology model of Ae4. [50]等排丝氨酸和半胱氨酸残基之间的环境是否不同？某些环境会促进胱氨酸 S-S 键的形成吗？随着水不溶性膜蛋白结构数据的日益普及，可溶性和膜蛋白之间的这些残基是否存在环境差异？丝氨酸和半胱氨酸残基周围的环境截然不同：丝氨酸残基约 50% 暴露在溶剂中，而半胱氨酸仅暴露 10%；后者更多地参与疏水相互作用，尽管存在骨架角度依赖性差异。 [1] 在人和鱼 PLK 同源物中，对应于 TbPLK Thr125 的丝氨酸残基的去磷酸化也降低了激酶活性，证明了在细胞周期中精确调节 PLK 活性的这一重要机制的保守性。 [2] 我们提出，NBCe1 丝氨酸残基的上下文依赖性和 mTOR 介导的多位点磷酸化可能是一种有效机制，有助于星形胶质细胞在病理生理条件下对酸/碱挑战的反应。 [3] 醇脱氢酶中该位置的苏氨酸或丝氨酸残基高度保守并且对催化有很大贡献。 [4] IKKβ 中激活环丝氨酸残基 (S177、S181) 的磷酸化是驱动肿瘤坏死因子 (TNF) α 诱导的 NF-κB 介导的基因表达的关键事件。 [5] 已知 Nedd4 家族的成员通过其多个 WW 结构域识别底物，这些结构域识别 PY 基序（PPxY、LPxY）或磷酸-苏氨酸或磷酸-丝氨酸残基。 [6] l-丝氨酸残基通过多个氢键位点选择性和残基特异性吸附在孔表面。 [7] 我们证明 PspA 与宿主衍生的 3-磷酸甘油醛脱氢酶 (GAPDH) 结合，该酶与垂死宿主细胞上的向外翻转的磷脂酰丝氨酸残基结合。 [8] 最近，组蛋白 PARylation 因子 (HPF1) 被证明是 PARP1 活性的关键调节剂，通过促进组蛋白的 PARylation 并将目标氨基酸特异性从酸性转向丝氨酸残基。 [9] NRAMP1 胞质暴露的 N 末端中磷酸化丝氨酸残基 20、22 和 24 的突变会改变其膜分布。 [10] 该资源揭示了糖基化只发生在丝氨酸残基上，并且糖蛋白/糖基化位点在 294 个可公开获得的芽孢杆菌中高度保守。 [11] 在这里，我们报告了一种高效且模块化的半合成途径的开发，该途径以化学方式安装在特定的丝氨酸残基上，以制备全长 ADP 核糖基化组蛋白 H3 和 H2B。 [12] 具体而言，我们将 PARP1 中的三个丝氨酸残基（499、507 和 519）确定为关键位点，其有效的 HPF1 依赖性修饰可对抗 PARP1 捕获并有助于抑制剂耐受性。 [13] 我们显示肌醇焦磷酸 5-IP7 将其高能 β 磷酸部分转移到 MYC 中央 PEST 域中的预磷酸化丝氨酸残基。 [14] 表明酵母 Gγ 亚基 Ste18 的 N 末端区域在一个本质上无序的区域内含有两个丝氨酸残基，这些残基被不同的激酶磷酸化以响应不同的刺激。 [15] 肌萎缩侧索硬化症 (ALS) 和额颞叶痴呆 (FTD) 中的主要聚集蛋白 RNA 结合蛋白 TDP-43 在疾病中的几个 C 末端丝氨酸残基上被过度磷酸化，这通常被认为促进 TDP-43 聚集。 [16] 这种寄生虫通过大量表达丝氨酸残基并产生混合的Alike/Tn结构来劫持宿主的生理A样/Tn形成，从而打破物种屏障，在人类血型O(H)中，这种结构受到种系编码的非免疫多反应性免疫球蛋白的攻击M (IgM)，发挥高度抗 A/B/H 侵袭性异凝集素活性。 [17] 其中，1332和1346位氨基酸的两个丝氨酸残基（S1332和S1346）在人HeLa细胞中肯定被磷酸化，而其他两个丝氨酸残基（S1616和S1691）没有被磷酸化。 [18] 白藜芦醇促进了我们首次报道的 LKB1 和 Sirt1 之间的结合，这种结合导致 LKB1 介导的 Sirt1 在 Sirt1 C 末端的三个不同丝氨酸残基处的磷酸化。 [19] 方法进行定点诱变以产生在308-325 aa区域中缺乏三个丝氨酸残基（Ser 316、Ser 320和Ser 321）的Che-1突变体（Che-1 3S）。 [20] 我们表明 AMPK 介导 TFEB 和 TFE3 在三个丝氨酸残基上的磷酸化，导致 TFEB/TFE3 在营养饥饿、FLCN 消耗和 mTORC1 或 AMPK 的药理学操作时的转录活性。 [21] 我们还鉴定了 Nur77 的细胞因子依赖性反式激活所需的一系列丝氨酸残基。 [22] 为了在氨基糖苷腺苷酸转移酶中找到功能性剪接位点，我们采用了一种简化策略，专门研究天然半胱氨酸和丝氨酸残基的灵活性，我们首先验证了拆分赋予氨苄青霉素、卡那霉素、氯霉素和潮霉素抗性的酶。 [23] 三种不同的 Pd 复合物被掺入到两种不同的转基因酶变体中，一种包含所有天然半胱氨酸残基变为丝氨酸残基，另一种变体包括直接在催化丝氨酸 (Ser114Cys) 中的额外 Cys 突变。 [24] , 丝氨酸残基旨在接收 D-木糖分子以启动 HS 链)。 [25] 免疫沉淀和细胞表面生物素化的使用表明，DAT 在丝氨酸残基处被磷酸化，泛素化并通过 PKCβ 依赖性机制释放到晚期内体中。 [26] 虽然 Musashi 最能被表征为靶 mRNA 翻译的阻遏物，但我们已经证明 Musashi 可以通过两个进化上保守的 C 末端丝氨酸残基上的调节磷酸化以细胞环境特异性方式激活靶 mRNA 翻译。 [27] 根据C末端保守的丝氨酸残基，所有ACS基因可分为三组，由外显子-内含子组织和保守基序分布支持。 [28] HPF1 与 PARP1 的结合控制了 ADP-核糖部分嫁接在 DNA 损伤附近蛋白质的丝氨酸残基上，主要是 PARP1 和组蛋白。 [29] 蛋白聚糖 (PG) 是具有糖胺聚糖 (GAG) 链的蛋白质，例如硫酸软骨素 (CS) 或硫酸乙酰肝素 (HS)，与丝氨酸残基相连。 [30] 该研究预测了 S1 菌株中蛋白酶羧肽酶 A1 的丝氨酸残基上有 19 个磷酸化位点。 [31] Alt-RPL36 包含四个磷酸丝氨酸残基，其点突变消除了与 TMEM24 的相互作用，因此，alt-RPL36 对 PI3K 信号传导和细胞大小的影响。 [32] STAT5a 丝氨酸残基 S726 和 S780 的磷酸化可以调节 STAT5a，从而成为这种二元性的基础。 [33] 菌膜以长链霉菌酸为代表，这些酸被各种受体酯化，包括： (1) 海藻糖，形成海藻糖单霉菌酸酯和二霉菌酸酯； (2) 阿拉伯半乳聚糖，形成阿拉伯半乳聚糖连接的分枝菌酸盐； (3) 在某些物种中，蛋白质丝氨酸残基，形成 O-mycoloylated 蛋白质。 [34] 高尔基连接蛋白 GRASP55 和 GRASP65 在多个丝氨酸残基上被 PR 泛素化，从而阻止了它们聚集和形成寡聚结构的能力。 [35] 舍拉莫利特同系物由两个 L-丝氨酸残基（环状或开环）的肽部分组成，这些残基连接到两条脂肪酸链（长度为 C10、C12 或 C12:1）。 [36] 通过质谱分析，我们在小鼠直系同源物的 N 末端（S26、S29、S541 和 S542）中鉴定了四个丝氨酸残基。 [37] 先前对酯酶机制的研究表明，酯酶的活性位点含有丝氨酸残基，通过对底物的亲核攻击来催化反应。 [38] 在 DNA 损伤修复过程中，PARP1 和 PARP2 与辅助因子 HPF1 结合，这是修饰丝氨酸残基上靶蛋白所必需的。 [39] 尽管 CRTC 中的三个保守丝氨酸残基与它们的磷酸化调节有关，但它们如何介导与 14-3-3 的相互作用尚不清楚。 [40] 已知 Nth1 在四个丝氨酸残基上被代谢激酶 PKA 磷酸化，在一个残基上被细胞周期激酶 CDK 磷酸化。 [41] 虽然未磷酸化的丝氨酸残基不直接与 ERK2 相互作用，但磷酸化的 Ser-116 与 FADD DED 上的精氨酸残基发生强烈的相互作用。 [42] PDHA1 含有三个丝氨酸残基，它们可以被四个抑制性丙酮酸脱氢酶激酶 (PDHK1-4) 和两个再活化磷酸酶 (PDP1,2) 的专用家族可逆地磷酸化。 [43] GIV 在人和鼠精子中的关键酪氨酸和丝氨酸残基上被快速磷酸调节。 [44] 分析了 HSP27、OSR1 和 MARCKS 的特定丝氨酸残基的磷酸化，以及由 FPR2 刺激激活的相应上游激酶。 [45] 最初有人提出，Wnts 在其保守的半胱氨酸和丝氨酸残基（mWnt3a 中的 C77 和 S209）处进行了脂质修饰，并且任一残基的突变都会阻碍其分泌和活性。 [46] 我们还发现干扰素治疗降低了这些丝氨酸残基的磷酸化水平，并概述了一种稳态调节机制，其中通过磷酸化抑制 MX2 以及 MLCP 介导的去磷酸化，平衡了 MX2 对正常细胞功能的有害影响与对 HIV 的先天免疫-1。 [47] 重要的是，我们发现 circGNG7 可以与功能性热休克蛋白 27 (HSP27) 的丝氨酸残基 78 和 82 结合，占据其磷酸化位点并阻碍其磷酸化，从而降低 HSP27-JNK/P38 丝裂原活化蛋白激酶 (MAPK) 的致癌性发信号。 [48] CK1 和 CK2 对丝氨酸残基的磷酸化调节其细胞内定位及其对激酶或磷酸酶的敏感性。 [49] 根据 Ae4 的同源模型，Ae4 序列分析显示两个潜在的 PKA 磷酸化丝氨酸残基位于细胞内 N 端结构域。 [50]
Three Serine Residues
Specifically, we identify three serine residues within PARP1 (499, 507, and 519) as key sites whose efficient HPF1-dependent modification counters PARP1 trapping and contributes to inhibitor tolerance. [1] Methods Site-directed Mutagenesis was performed to generate a Che-1 mutant (Che-1 3S) lacking three serine residues (Ser 316 , Ser 320 and Ser 321 ) in 308–325 aa region. [2] We show that AMPK mediates phosphorylation of TFEB and TFE3 on three serine residues, leading to TFEB/TFE3 transcriptional activity upon nutrient starvation, FLCN depletion and pharmacological manipulation of mTORC1 or AMPK. [3] PDHA1 contains three serine residues that can be reversibly phosphorylated by a dedicated family of four inhibitory pyruvate dehydrogenase kinases (PDHK1-4) and two reactivating phosphatases (PDP1,2). [4] Methods: Site-directed Mutagenesis was performed to generate a Che-1 mutant (Che-1 3S) lacking three serine residues (Ser, Ser and Ser) in 308–325 aa region. [5] Once an oocyte resumes meiosis, activated CDK1 and ERK1/2 cooperatively mediate the phosphorylation of three serine residues of PAPα, 537, 545 and 558, thereby leading to increased activity. [6] We show that AMPK mediates phosphorylation of TFEB and TFE3 on three serine residues, leading to TFEB and TFE3 transcriptional activity upon nutrient starvation, FLCN (folliculin) depletion and pharmacological manipulation of MTORC1 or AMPK. [7] The goal of this study was to examine the role of three serine residues in the large cytoplasmic loop of the &agr;4 subunit on &agr;4&bgr;2* upregulation in neurons. [8] A peptide comprising the juxtamembrane C‐terminal intracellular loop 4 (IL4) of the CB1 cannabinoid receptor possesses three serine residues (Ser402, Ser411, and Ser415). [9]具体而言，我们将 PARP1 中的三个丝氨酸残基（499、507 和 519）确定为关键位点，其有效的 HPF1 依赖性修饰可对抗 PARP1 捕获并有助于抑制剂耐受性。 [1] 方法进行定点诱变以产生在308-325 aa区域中缺乏三个丝氨酸残基（Ser 316、Ser 320和Ser 321）的Che-1突变体（Che-1 3S）。 [2] 我们表明 AMPK 介导 TFEB 和 TFE3 在三个丝氨酸残基上的磷酸化，导致 TFEB/TFE3 在营养饥饿、FLCN 消耗和 mTORC1 或 AMPK 的药理学操作时的转录活性。 [3] PDHA1 含有三个丝氨酸残基，它们可以被四个抑制性丙酮酸脱氢酶激酶 (PDHK1-4) 和两个再活化磷酸酶 (PDP1,2) 的专用家族可逆地磷酸化。 [4] nan [5] nan [6] nan [7] nan [8] nan [9]
Specific Serine Residues
Here, we report the development of an efficient and modular semisynthetic route to full-length ADP-ribosylated histones H3 and H2B, chemically installed at specific serine residues. [1] Phosphorylation at specific serine residues of HSP27, OSR1, and MARCKS, as well as the respective upstream kinases activated by FPR2 stimulation was analysed. [2] CPPED1 dephosphorylated specific serine residues in PAK4, while phosphorylation levels in PIK3R2 remained unchanged. [3] 32 min, we mutated specific serine residues that we identified as potentially relevant through structure comparison with thermophilic CelA from Clostridium thermocellum. [4] A vital step in IRF3 activation is phosphorylation of specific serine residues initiating a conformational change, dimerization and exposure of nuclear localization signal and DNA binding domain. [5] Binding of Rom2p to the cytoplasmic tail of Wsc1p requires dephosphorylation of specific serine residues but the mechanism by which the sensor is dephosphorylated and how it subsequently interacts with Rom2p remains unclear. [6] Using experiments designed to probe distinct dynamic modes, we identify regions with varying mobilities within HP1α molecules and show that specific serine residues uniquely contribute to gel formation. [7]在这里，我们报告了一种高效且模块化的半合成途径的开发，该途径以化学方式安装在特定的丝氨酸残基上，以制备全长 ADP 核糖基化组蛋白 H3 和 H2B。 [1] 分析了 HSP27、OSR1 和 MARCKS 的特定丝氨酸残基的磷酸化，以及由 FPR2 刺激激活的相应上游激酶。 [2] nan [3] nan [4] nan [5] nan [6] nan [7]
Phosphorylated Serine Residues
Mutation of the phosphorylated serine residues 20, 22 and 24 in the cytosol-exposed N-terminus of NRAMP1 alters its membrane distribution. [1] We show that the inositol pyrophosphate 5-IP7 transfers its high-energy beta phosphate moiety to pre-phosphorylated serine residues in the central PEST domain of MYC. [2] Comparing results with the most common genetic variant αS1-CN C, αS1-CN E variant showed a reduced number of phosphorylated serine residues (αS1-CN E -4P versus αS1-CN C -9P) and a lower measured molecular mass (22241. [3] Furthermore, the presence of the phosphorylated serine residues is demonstrated to have a shielding effect during deprotonation of the protein. [4]NRAMP1 胞质暴露的 N 末端中磷酸化丝氨酸残基 20、22 和 24 的突变会改变其膜分布。 [1] 我们显示肌醇焦磷酸 5-IP7 将其高能 β 磷酸部分转移到 MYC 中央 PEST 域中的预磷酸化丝氨酸残基。 [2] nan [3] nan [4]
Terminal Serine Residues
The major aggregating protein in amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), the RNA-binding protein TDP-43, is hyperphosphorylated in disease on several C-terminal serine residues, which is generally believed to promote TDP-43 aggregation. [1] While Musashi is best characterized as a repressor of target mRNA translation, we have shown that Musashi can activate target mRNA translation in a cell context specific manner via regulatory phosphorylation on two evolutionarily conserved C-terminal serine residues. [2] This de-repression does not require regulatory phosphorylation of Musashi on two conserved C-terminal serine residues. [3] Here, we show that fission yeast DDK/Hsk1 phosphorylates sirtuin, Hst4 upon replication stress at C-terminal serine residues. [4]肌萎缩侧索硬化症 (ALS) 和额颞叶痴呆 (FTD) 中的主要聚集蛋白 RNA 结合蛋白 TDP-43 在疾病中的几个 C 末端丝氨酸残基上被过度磷酸化，这通常被认为促进 TDP-43 聚集。 [1] 虽然 Musashi 最能被表征为靶 mRNA 翻译的阻遏物，但我们已经证明 Musashi 可以通过两个进化上保守的 C 末端丝氨酸残基上的调节磷酸化以细胞环境特异性方式激活靶 mRNA 翻译。 [2] nan [3] nan [4]
Two Serine Residues
showed that the N-terminal region of the yeast Gγ subunit Ste18 contains two serine residues within an intrinsically disordered region that were phosphorylated by different kinases in response to distinct stimuli. [1] Among them, two serine residues at amino acid positions 1332 and 1346 (S1332 and S1346) were certainly phosphorylated in human HeLa cells, but other two serine residues (S1616 and S1691) were not phosphorylated. [2] Full activation requires phosphorylation of two serine residues of INCENP that are conserved through evolution, although the mechanism of this activation has not been explained. [3]表明酵母 Gγ 亚基 Ste18 的 N 末端区域在一个本质上无序的区域内含有两个丝氨酸残基，这些残基被不同的激酶磷酸化以响应不同的刺激。 [1] 其中，1332和1346位氨基酸的两个丝氨酸残基（S1332和S1346）在人HeLa细胞中肯定被磷酸化，而其他两个丝氨酸残基（S1616和S1691）没有被磷酸化。 [2] nan [3]
Conserved Serine Residues
According to the conserved serine residues at C-terminal, all the ACS genes could be characterized into three groups, which were supported by the exon-intron organizations and conserved motif distributions. [1] Although three conserved serine residues in CRTCs have been implicated in their phosphorylation regulation, how they mediate interactions with 14-3-3 is unclear. [2] This study joins our previous efforts to elucidate how NS5A transits between hypo- and hyperphosphorylated states via phosphorylation on a series of highly conserved serine residues. [3]根据C末端保守的丝氨酸残基，所有ACS基因可分为三组，由外显子-内含子组织和保守基序分布支持。 [1] 尽管 CRTC 中的三个保守丝氨酸残基与它们的磷酸化调节有关，但它们如何介导与 14-3-3 的相互作用尚不清楚。 [2] nan [3]
3 Serine Residues
Here, for the first time, we show that insulin-induced phosphorylation of these 3 serine residues mainly impinged on the mechanisms of proteostasis of both full-length and mature SREBP-1c in the McArdle-RH7777 hepatoma cells. [1] A knockin rat model harboring mutations of the last 3 serine residues of the &bgr;1AR C terminus, a component of the putative &bgr;arr1 binding site and GRK2 phosphorylation site, eliminated the offside compartmentalization conferred by &bgr;2AR activation. [2]Fmy Serine Residues
By mass spectrometry, we identified four serine residues within the N-terminus (S26, S29, S541, and S542) constitutively phosphorylated in the mouse ortholog. [1] Nth1 is known to be phosphorylated by the metabolic kinase PKA on four serine residues and by the cell cycle kinase CDK on one residue. [2]通过质谱分析，我们在小鼠直系同源物的 N 末端（S26、S29、S541 和 S542）中鉴定了四个丝氨酸残基。 [1] 已知 Nth1 在四个丝氨酸残基上被代谢激酶 PKA 磷酸化，在一个残基上被细胞周期激酶 CDK 磷酸化。 [2]
serine residues within
Specifically, we identify three serine residues within PARP1 (499, 507, and 519) as key sites whose efficient HPF1-dependent modification counters PARP1 trapping and contributes to inhibitor tolerance. [1] showed that the N-terminal region of the yeast Gγ subunit Ste18 contains two serine residues within an intrinsically disordered region that were phosphorylated by different kinases in response to distinct stimuli. [2] By mass spectrometry, we identified four serine residues within the N-terminus (S26, S29, S541, and S542) constitutively phosphorylated in the mouse ortholog. [3] Purified BB0562 demonstrated lipolytic activity dependent on the catalytic serine residues within the two motifs. [4] Using an antibody that recognizes phospho-serine residues within the consensus sequence phosphorylated by PKC, we analyzed the 1-dimensional banding profile of PKC substrate protein phosphorylation from the Neuro2A mouse neuroblastoma cell line. [5] Hyperphosphorylation occurs primarily at six serine residues within the low complexity sequence I of NS5A. [6]具体而言，我们将 PARP1 中的三个丝氨酸残基（499、507 和 519）确定为关键位点，其有效的 HPF1 依赖性修饰可对抗 PARP1 捕获并有助于抑制剂耐受性。 [1] 表明酵母 Gγ 亚基 Ste18 的 N 末端区域在一个本质上无序的区域内含有两个丝氨酸残基，这些残基被不同的激酶磷酸化以响应不同的刺激。 [2] 通过质谱分析，我们在小鼠直系同源物的 N 末端（S26、S29、S541 和 S542）中鉴定了四个丝氨酸残基。 [3] nan [4] nan [5] nan [6]
serine residues located
Ae4 sequence analysis showed two potential PKA phosphorylation serine residues located at the intracellular N-terminal domain according to a homology model of Ae4. [1] Specifically, we discovered that NLK associates with Smad3 and phosphorylates the designated serine residues located in the linker region of Smad2 and Smad3, which inhibits phosphorylation at the C terminus, thereby decreasing the duration of TGF-β signaling. [2]根据 Ae4 的同源模型，Ae4 序列分析显示两个潜在的 PKA 磷酸化丝氨酸残基位于细胞内 N 端结构域。 [1] 具体来说，我们发现 NLK 与 Smad3 结合并磷酸化位于 Smad2 和 Smad3 接头区域的指定丝氨酸残基，从而抑制 C 末端的磷酸化，从而减少 TGF-β 信号传导的持续时间。 [2]