Modified SH2 domain to phototrap and identify phosphotyrosine proteins from subcellular sites within cells

Akiyoshi Uezu; Hirokazu Okada; Hideji Murakoshi; Cosmo D. del Vescovo; Ryohei Yasuda; Dario Diviani; Scott H. Soderling

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Modified SH2 domain to phototrap and identify phosphotyrosine proteins from subcellular sites within cells

机译：修饰的SH2结构域可从细胞内的亚细胞部位捕获并鉴定磷酸酪氨酸蛋白

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Reversible protein phosphoryla-tion (i.e., the addition or removal of a phosphate group to or from a molecule, such as a protein) is used to govern almost every cellular event. Tightly controlling this essential process is the coordinated interplay between PKs, which add the phosphate groups, and phosphatases, which remove them (1). For achieving specific cellular responses, phosphoryla-tion signaling pathways are both spatially and temporally modulated within the cell. Indeed, many cellular proteins are controlled by reversible phosphory-lation within distinct subcellular sites to enable extracellular cues to be interpreted and translated into appropriate cell responses.

机译：可逆的蛋白质磷酸化作用（即，在一个分子（例如蛋白质）中添加或去除一个分子上的磷酸基）被用于控制几乎所有的细胞事件。严格控制这一基本过程的是PK之间的协调相互作用，PK之间增加了磷酸基团，而磷酸酶去除了它们（1）。为了实现特定的细胞应答，磷酸化信号传导途径在细胞内在空间和时间上均得到调节。实际上，许多细胞蛋白受不同亚细胞位点内可逆的磷酸化作用的控制，以使细胞外信号能够被解释并转化为适当的细胞反应。

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《Proceedings of the National Academy of Sciences of the United States of America》 |2012年第43期|17323-17324|共2页
作者
Akiyoshi Uezu; Hirokazu Okada; Hideji Murakoshi; Cosmo D. del Vescovo; Ryohei Yasuda; Dario Diviani; Scott H. Soderling;
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作者单位

Department of Cell Biology, Duke University Medical School, Durham, NC 27710;

Department of Cell Biology, Duke University Medical School, Durham, NC 27710;

Howard Hughes Medical Institute and Neurobiology Department, Duke University Medical School, Durham, NC 27710,Supportive Center for Brain Research, National Institute for Physiological Science and the Graduate University for Advanced Studies (SOKENDAI), Myodaiji, Okazaki 444-8585, Japan;

Department of Pharmacology and Toxicology, University of Lausanne, 1005 Lausanne, Switzerland;

Howard Hughes Medical Institute and Neurobiology Department, Duke University Medical School, Durham, NC 27710;

Department of Pharmacology and Toxicology, University of Lausanne, 1005 Lausanne, Switzerland;

Department of Cell Biology, Duke University Medical School, Durham, NC 27710;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
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正文语种 eng
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1. Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins. [J] . E N Neumeister, Y Zhu, S Richard, Molecular and Cellular Biology . 1995,第6期

机译：ZAP-70与磷酸化T细胞受体zeta和eta的结合可增强其自身磷酸化作用，并为含SH2域的蛋白质产生特异性结合位点。
2. The sites of phosphorylation by protein kinase C and an intact SH2 domain are required for the enhanced response to beta-adrenergic agonists in cells overexpressing c-src. [J] . J S Moyers, A H Bouton, S J Parsons Molecular and Cellular Biology . 1993,第4期

机译：在过表达c-src的细胞中，对β-肾上腺素能激动剂的增强反应需要蛋白激酶C和完整的SH2结构域的磷酸化位点。
3. Tyrosine 192 within the SH2 domain of the Src-protein tyrosine kinase p56 Lck regulates T-cell activation independently of Lck/CD45 interactions [J] . Matthias K?stle, Camilla Merten, Roland Hartig, Cell Communication and Signaling . 2020,第1期

机译：SRC-蛋白酪氨酸激酶P56 LCK的SH2结构域内的酪氨酸192调节T细胞活化，独立于LCK / CD45相互作用
4. A Triad of Lys12, Lys41, Arg78 Spatial Domain, a Novel Identified Heparin Binding Site on Tat Protein, Facilitates Tat-Driven Cell Adhesion [C] . Jing Ai, Xianliang Xin, Mingyue Zheng, 第四届国际分子模拟与信息技术应用学术会议（The 4th International Conference of Molecular Simulations and Applied Informatics Technologies）论文集 . 2008

机译：三联体Lys12，Lys41，Arg78空间结构域，在Tat蛋白上新鉴定的肝素结合位点，促进了Tat驱动的细胞粘附
5. Identification of SH2 -domain containing protein tyrosine phosphatase SHP-2 targets in physiological and pathophysiological cell signaling [D] . Eminaga, Seda 2007

机译：生理和病理生理细胞信号转导中含有SH2结构域的蛋白酪氨酸磷酸酶SHP-2靶标的鉴定
6. PNAS Plus: Modified SH2 domain to phototrap and identify phosphotyrosine proteins from subcellular sites within cells [O] . Akiyoshi Uezu, Hirokazu Okada, Hideji Murakoshi, 2012

机译：PNAS Plus：经过修饰的SH2结构域可从细胞内的亚细胞部位捕获并鉴定磷酸酪氨酸蛋白
7. Binding of ZAP-70 to phosphorylated T-cell receptor zeta and eta enhances its autophosphorylation and generates specific binding sites for SH2 domain-containing proteins. [O] . Neumeister, E N, Zhu, Y, Richard, S, 1995

机译：ZAP-70与磷酸化T细胞受体zeta和eta的结合增强了其自身磷酸化作用，并为含SH2域的蛋白质生成了特异性结合位点。

Modified SH2 domain to phototrap and identify phosphotyrosine proteins from subcellular sites within cells

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