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Online-Ressource

Atlas of Mineral Deposits Distribution in China (2020) (2021)

Qi, Fanyu [VerfasserIn]

Singapore : Springer Singapore | Singapore : Imprint: Springer

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Schlagwort(e): Geology. ; Mineralogy. ; Earth sciences. ; Atlas ; China ; Erzlagerstätte ; Bitumenlagerstätte ; Naturstein ; Industriemineral ; Kohlenlagerstätte ; China ; Mineralischer Rohstoff ; Lagerstätte ; Vorkommen

Beschreibung / Inhaltsverzeichnis: This open access book includes instruction of national mineral database 2020 and atlas of national mineral deposits distribution derived from national mineral database 2020. National mineral database 2020 is based on data from National Geological Archives China(NGAC). Moreover, it introduces the construction method and updates maintenance mechanism of the mineral deposits database and proposes the concept of updating data based on collected archives. The construction guideline on national mineral deposits database provides guiding framework for the future development on geological database. .

Materialart: Online-Ressource

Seiten: 1 Online-Ressource(VII, 93 p. 90 illus., 89 illus. in color.)

Ausgabe: 1st ed. 2021.

ISBN: 9789811609725

Serie: The China Geological Survey Series

URL: https://doi.org/10.1007/978-981-16-0972-5

DOI: 10.1007/978-981-16-0972-5

Sprache: Englisch

Anmerkung: Open Access

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Allosteric modulation of the catalytic VYD loop in Slingshot by its N-terminal domain underlies both Slingshot auto-inhibition and activation [Protein Structure and Folding] (2018)

Duxiao Yang, Peng Xiao, Qing Li, Xiaolei Fu, Chang Pan, Di Lu, Shishuai Wen, Wanying Xia, Dongfang He, Hui Li, Hao Fang, Yuemao Shen, Zhigang Xu, Amy Lin, Chuan Wang, Xiao Yu, Jiawei Wu, Jinpeng Sun

The American Society for Biochemistry and Molecular Biology (ASBMB)

In: Journal of Biological Chemistry

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Publikationsdatum: 2018-10-20

Beschreibung: Slingshots are phosphatases that modulate cytoskeleton dynamics, and their activities are tightly regulated in different physiological contexts. Recently, abnormally elevated Slingshot activity has been implicated in many human diseases, such as cancer, Alzheimer's disease, and vascular diseases. Therefore, Slingshot-specific inhibitors have therapeutic potential. However, an enzymological understanding of the catalytic mechanism of Slingshots and of their activation by actin is lacking. Here, we report that the N-terminal region of human Slingshot2 auto-inhibits its phosphatase activity in a noncompetitive manner. pH-dependent phosphatase assays and leaving-group dependence studies suggested that the N-terminal domain of Slingshot2 regulates the stability of the leaving group of the product during catalysis by modulating the general acid Asp361 in the catalytic VYD loop. F-actin binding relieved this auto-inhibition and restored the function of the general acid. Limited tryptic digestion and biophysical studies identified large conformational changes in Slingshot2 after the F-actin binding. The dissociation of N-terminal structural elements, including Leu63, and the exposure of the loop between α-helix-2 and β-sheet-3 of the phosphatase domain served as the structural basis for Slingshot activation via F-actin binding in vitro and via neuregulin stimulation in cells. Moreover, we designed a FlAsH-BRET–based Slingshot2 biosensor whose readout was highly correlated with the in vivo phosphatase activities of Slingshot2. Our results reveal the auto-inhibitory mechanism and allosteric activation mechanisms of a human Slingshot phosphatase. They also contribute to the design of new strategies to study Slingshot regulation in various cellular contexts and to screen for new activators/inhibitors of Slingshot activity.

Print ISSN: 0021-9258

Digitale ISSN: 1083-351X

Thema: Biologie , Chemie und Pharmazie

Publiziert von The American Society for Biochemistry and Molecular Biology (ASBMB)

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