Relevant bibliographies by topics / SgK269

Academic literature on the topic 'SgK269'

Author: Grafiati
Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "SgK269"

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O'Rourke, Rachelle L., and Roger J. Daly. "The pseudokinases SgK269 and SgK223: A novel oncogenic alliance in human cancer." Cell Adhesion & Migration 12, no. 6 (December 21, 2017): 524–28. http://dx.doi.org/10.1080/19336918.2017.1394570.

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Liu, Ling, Yu Wei Phua, Rachel S. Lee, Xiuquan Ma, Yiping Jenkins, Karel Novy, Emily S. Humphrey, et al. "Homo- and Heterotypic Association Regulates Signaling by the SgK269/PEAK1 and SgK223 Pseudokinases." Journal of Biological Chemistry 291, no. 41 (August 16, 2016): 21571–83. http://dx.doi.org/10.1074/jbc.m116.748897.

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Lopez, Mitchell L., Megan Lo, Jennifer E. Kung, Małgorzata Dudkiewicz, Gwendolyn M. Jang, John Von Dollen, Jeffrey R. Johnson, Nevan J. Krogan, Krzysztof Pawłowski, and Natalia Jura. "PEAK3/C19orf35 pseudokinase, a new NFK3 kinase family member, inhibits CrkII through dimerization." Proceedings of the National Academy of Sciences 116, no. 31 (July 16, 2019): 15495–504. http://dx.doi.org/10.1073/pnas.1906360116.

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Members of the New Kinase Family 3 (NKF3), PEAK1/SgK269 and Pragmin/SgK223 pseudokinases, have emerged as important regulators of cell motility and cancer progression. Here, we demonstrate that C19orf35 (PEAK3), a newly identified member of the NKF3 family, is a kinase-like protein evolutionarily conserved across mammals and birds and a regulator of cell motility. In contrast to its family members, which promote cell elongation when overexpressed in cells, PEAK3 overexpression does not have an elongating effect on cell shape but instead is associated with loss of actin filaments. Through an unbiased search for PEAK3 binding partners, we identified several regulators of cell motility, including the adaptor protein CrkII. We show that by binding to CrkII, PEAK3 prevents the formation of CrkII-dependent membrane ruffling. This function of PEAK3 is reliant upon its dimerization, which is mediated through a split helical dimerization domain conserved among all NKF3 family members. Disruption of the conserved DFG motif in the PEAK3 pseudokinase domain also interferes with its ability to dimerize and subsequently bind CrkII, suggesting that the conformation of the pseudokinase domain might play an important role in PEAK3 signaling. Hence, our data identify PEAK3 as an NKF3 family member with a unique role in cell motility driven by dimerization of its pseudokinase domain.
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Croucher, David R., Falko Hochgräfe, Luxi Zhang, Ling Liu, Ruth J. Lyons, Danny Rickwood, Carole M. Tactacan, et al. "Involvement of Lyn and the Atypical Kinase SgK269/PEAK1 in a Basal Breast Cancer Signaling Pathway." Cancer Research 73, no. 6 (February 1, 2013): 1969–80. http://dx.doi.org/10.1158/0008-5472.can-12-1472.

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Yoshida-Moriguchi, Takako, Tobias Willer, Mary E. Anderson, David Venzke, Tamieka Whyte, Francesco Muntoni, Hane Lee, Stanley F. Nelson, Liping Yu, and Kevin P. Campbell. "SGK196 Is a Glycosylation-Specific O-Mannose Kinase Required for Dystroglycan Function." Science 341, no. 6148 (August 8, 2013): 896–99. http://dx.doi.org/10.1126/science.1239951.

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Phosphorylated O-mannosyl trisaccharide [N-acetylgalactosamine–β3-N-acetylglucosamine–β4-(phosphate-6-)mannose] is required for dystroglycan to bind laminin-G domain–containing extracellular proteins with high affinity in muscle and brain. However, the enzymes that produce this structure have not been fully elucidated. We found that glycosyltransferase-like domain–containing 2 (GTDC2) is a protein O-linked mannose β 1,4-N-acetylglucosaminyltransferase whose product could be extended by β 1,3-N-acetylgalactosaminyltransferase2 (B3GALNT2) to form the O-mannosyl trisaccharide. Furthermore, we identified SGK196 as an atypical kinase that phosphorylated the 6-position of O-mannose, specifically after the mannose had been modified by both GTDC2 and B3GALNT2. These findings suggest how mutations in GTDC2, B3GALNT2, and SGK196 disrupt dystroglycan receptor function and lead to congenital muscular dystrophy.
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Pao, Alan C., Aditi Bhargava, Francesca Di Sole, Raymond Quigley, Xinli Shao, Jian Wang, Sheela Thomas, et al. "Expression and role of serum and glucocorticoid-regulated kinase 2 in the regulation of Na+/H+ exchanger 3 in the mammalian kidney." American Journal of Physiology-Renal Physiology 299, no. 6 (December 2010): F1496—F1506. http://dx.doi.org/10.1152/ajprenal.00075.2010.

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Serum and glucocorticoid-regulated kinase 2 (sgk2) is 80% identical to the kinase domain of sgk1, an important mediator of mineralocorticoid-regulated sodium (Na+) transport in the distal nephron of the kidney. The expression pattern and role in renal function of sgk2 are virtually uncharacterized. In situ hybridization and immunohistochemistry of rodent kidney coupled with real-time RT-PCR of microdissected rat kidney tubules showed robust sgk2 expression in the proximal straight tubule and thick ascending limb of the loop of Henle. Sgk2 expression was minimal in distal tubule cells with aquaporin-2 immunostaining but significant in proximal tubule cells with Na+/H+ exchanger 3 (NHE3) immunostaining. To ascertain whether mineralocorticoids regulate expression of sgk2 in a manner similar to sgk1, we examined sgk2 mRNA expression in the kidneys of adrenalectomized rats treated with physiological doses of aldosterone together with the glucocorticoid receptor antagonist RU486. Northern blot analysis and in situ hybridization showed that, unlike sgk1, sgk2 expression in the kidney was not altered by aldosterone treatment. Based on the observation that sgk2 is expressed in proximal tubule cells that also express NHE3, we asked whether sgk2 regulates NHE3 activity. We heterologously expressed sgk2 in opossum kidney (OKP) cells and measured Na+/H+ exchange activity by Na+-dependent cell pH recovery. Constitutively active sgk2, but not sgk1, stimulated Na+/H+ exchange activity by >30%. Moreover, the sgk2-mediated increase in Na+/H+ exchange activity correlated with an increase in cell surface expression of NHE3. Together, these results suggest that the pattern of expression, regulation, and role of sgk2 within the mammalian kidney are distinct from sgk1 and that sgk2 may play a previously unrecognized role in the control of transtubular Na+ transport through NHE3 in the proximal tubule.
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Ranzuglia, Valentina, Ilaria Lorenzon, Ilenia Pellarin, Maura Sonego, Alessandra Dall’Acqua, Sara D’Andrea, Sara Lovisa, et al. "Serum- and glucocorticoid- inducible kinase 2, SGK2, is a novel autophagy regulator and modulates platinum drugs response in cancer cells." Oncogene 39, no. 40 (August 27, 2020): 6370–86. http://dx.doi.org/10.1038/s41388-020-01433-6.

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Abstract For many tumor types chemotherapy still represents the therapy of choice and many standard treatments are based on the use of platinum (PT) drugs. However, de novo or acquired resistance to platinum is frequent and leads to disease progression. In Epithelial Ovarian Cancer (EOC) patients, PT-resistant recurrences are very common and improving the response to treatment still represents an unmet clinical need. To identify new modulators of PT-sensitivity, we performed a loss-of-function screening targeting 680 genes potentially involved in the response of EOC cells to platinum. We found that SGK2 (Serum-and Glucocorticoid-inducible kinase 2) plays a key role in PT-response. We show here that EOC cells relay on the induction of autophagy to escape PT-induced death and that SGK2 inhibition increases PT sensitivity inducing a block in the autophagy cascade due to the impairment of lysosomal acidification. Mechanistically we demonstrate that SGK2 controls autophagy in a kinase-dependent manner by binding and inhibiting the V-ATPase proton pump. Accordingly, SGK2 phosphorylates the subunit V1H (ATP6V1H) of V-ATPase and silencing or chemical inhibition of SGK2, affects the normal autophagic flux and sensitizes EOC cells to platinum. Hence, we identified a new pathway that links autophagy to the survival of cancer cells under platinum treatment in which the druggable kinase SGK2 plays a central role. Our data suggest that blocking autophagy via SGK2 inhibition could represent a novel therapeutic strategy to improve patients’ response to platinum.
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KOBAYASHI, Takayasu, Maria DEAK, Nick MORRICE, and Philip COHEN. "Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase." Biochemical Journal 344, no. 1 (November 8, 1999): 189–97. http://dx.doi.org/10.1042/bj3440189.

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The catalytic domain of serum- and glucocorticoid-induced protein kinase (SGK) is 54% identical with protein kinase B (PKB) and, like PKB, is activated in vitro by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and in vivo in response to signals that activate phosphatidylinositol (PI) 3-kinase. Here we identify two novel isoforms of SGK, termed SGK2 and SGK3, whose catalytic domains share 80% amino acid sequence identity with each other and with SGK (renamed SGK1). Like SGK1, the mRNA encoding SGK3 is expressed in all tissues examined, but SGK2 mRNA is only present at significant levels in liver, kidney and pancreas and, at lower levels, in the brain. The levels of SGK2 mRNA in H4IIE cells and SGK3 mRNA in Rat2 fibroblasts are not increased by stimulation with serum or dexamethasone, whereas the level of SGK1 mRNA is increased greatly. SGK2 and SGK3 are activated in vitro by PDK1, albeit more slowly than SGK1, and their activation is accompanied by the phosphorylation of Thr193 and Thr253 respectively, the residues equivalent to the Thr in the ‘activation loop’ of PKB that is targeted by PDK1. The PDK1-catalysed phosphorylation and activation of SGK2 and SGK3, like SGK1, is greatly potentiated by mutating Ser356 and Ser419 respectively to Asp, these residues being equivalent to the C-terminal phosphorylation site of PKB. Like SGK1, SGK2 and SGK3 are activated 5-fold via a phosphorylation mechanism when cells are exposed to H2O2 but, in contrast with SGK1, activation is only suppressed partially by inhibitors of PI 3-kinase. SGK2 and SGK3 are activated to a smaller extent by insulin-like growth factor-1 (2-fold) than SGK1 (5-fold). Like PKB and SGK1, SGK2 and SGK3 preferentially phosphorylate Ser and Thr residues that lie in Arg-Xaa-Arg-Xaa-Xaa-Ser/Thr motifs.
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9

Ardicli, D., R. Gocmen, S. Cirak, B. Talim, G. Haliloglu, and H. Topaloglu. "Congenital mirror movements in alpha-dystroglycanopathy (ADG) due to SGK196 mutation." Neuromuscular Disorders 26 (October 2016): S165. http://dx.doi.org/10.1016/j.nmd.2016.06.287.

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10

He, Peijian, Sei-Jung Lee, Songbai Lin, Ursula Seidler, Florian Lang, Geza Fejes-Toth, Aniko Naray-Fejes-Toth, and C. Chris Yun. "Serum- and glucocorticoid-induced kinase 3 in recycling endosomes mediates acute activation of Na+/H+ exchanger NHE3 by glucocorticoids." Molecular Biology of the Cell 22, no. 20 (October 15, 2011): 3812–25. http://dx.doi.org/10.1091/mbc.e11-04-0328.

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Na+/H+ exchanger 3 (NHE3) is the major Na+ transporter in the intestine. Serum- and glucocorticoid-induced kinase (SGK) 1 interacts with NHE regulatory factor 2 (NHERF2) and mediates activation of NHE3 by dexamethasone (Dex) in cultured epithelial cells. In this study, we compared short-term regulation of NHE3 by Dex in SGK1-null and NHERF2-null mice. In comparison to wild-type mice, loss of SGK1 or NHERF2 significantly attenuated regulation of NHE3 by Dex but did not completely obliterate the effect. We show that transfection of SGK2 or SGK3 in PS120 cells resulted in robust activation of NHE3 by Dex. However, unlike SGK1 or SGK2, SGK3 rapidly activated NHE3 within 15 min of Dex treatment in both PS120 and Caco-2bbe cells. Immunofluorescence analysis showed that SGK3 colocalized with NHE3 in recycling endosomes, whereas SGK1 and SGK2 were diffusely distributed. Mutation of Arg-90 of SGK3 disrupted the endosomal localization of SGK3 and delayed NHE3 activation. Activation of SGK3 and NHE3 by Dex was dependent on phosphoinositide 3-kinase (PI3K) and phosphoinositide-dependent kinase 1 (PDK1), and Dex induced translocation of PDK1 to endosomes. Our study identifies SGK3 as a novel endosomal kinase that acutely regulates NHE3 in a PI3K-dependent mechanism.
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Dissertations / Theses on the topic "SgK269"

1

Yang, Ta-Hsin, and 仰大信. "The Study on the Performance Persistency of Hedge Fund by Behavioral Finance." Thesis, 2005. http://ndltd.ncl.edu.tw/handle/sgk2g4.

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碩士
朝陽科技大學
財務金融系碩士班
93
In this study, the persistence of hedge fund performance is examined. We find that the buying winners will obtain the abnormal returns at least 12 months before market information has not yet fully responded except some hedging strategies. Hedge fund is not a short-run tool of the investment. The losers of hedge fund will acquire the loss and show the persistence of performance. As we have a closer look at the 14 operation strategies, the performance of big-size hedge fund will stay in top-performing groups; meanwhile, the small-size fund will stay bottom-performance one. It shows that big-size hedge fund has momentum. In 14 kinds of operation strategies of hedge funds, the loser strategy and the winner strategy all have obvious persistence of performance, that is, there are abnormal returns for both. It shows that the hedge fund market is not efficient. After observing 14 kinds of strategy, we find no persistence of hedge fund’s performance and the phenomenon of reversal. The investor fails to catch reversal timing and direction through the volume of transaction. The investor can''t make track for the buy-high and sell-low strategy or the reversal strategy to obtain abnormal returns.
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Book chapters on the topic "SgK269"

1

"Sugen Kinase 496 (SgK496)." In Encyclopedia of Signaling Molecules, 5221. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_103701.

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Conference papers on the topic "SgK269"

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Liu, Ling, Howard Chan, David Croucher, Falco Hochgräfe, Luxi Zhang, Carole Tactacan, and Roger Daly. "Abstract 2507: Mechanistic and functional characterization of the atypical kinase SgK269/PEAK1 in breast cancer." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-2507.

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Tactacan, Carole M., Emily S. Humphrey, Andrew V. Biankin, and Roger J. Daly. "Abstract 4866: The atypical kinase SgK223 is a novel mediator of cell invasion in pancreatic cancer." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-4866.

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Pennington, Katie L., James Woods, Colin Muir, Colten M. McEwan, Pramoda S. Aththota Gamage, Riley J. Eastmond, Crissy M. Egbert, Tyler Heaton, Stephen R. Piccolo, and Joshua L. Andersen. "Abstract 2295: SGK2, 14-3-3, and HUWE1 coordinately regulate the localization and stability of PTOV1." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-2295.

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