Relevant bibliographies by topics / SgK223

Academic literature on the topic 'SgK223'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "SgK223"

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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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Glenn, Martha J., Rosalie G. Waller, and Nicola J. Camp. "Exome Sequencing in a Family with Chronic Lymphocytic Leukemia, Mantle Cell Lymphoma and Autoimmune Disease Uncovers Potential Germline Risk-Alleles." Blood 124, no. 21 (December 6, 2014): 5629. http://dx.doi.org/10.1182/blood.v124.21.5629.5629.

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Abstract We identified a Caucasian family with dense distribution of B-cell non-Hodgkin lymphoma (NHL) and autoimmune disease (Figure 1). Within the family, three siblings and their mother have B-cell NHL (three with chronic lymphocytic leukemia [CLL]; one with mantle cell lymphoma [MCL]), and four family members have autoimmune diseases (rheumatoid arthritis or multiple sclerosis). In addition, two family members have melanoma. To investigate the genetic factors involved in B-cell NHL in this family, we exome sequenced nine individuals, including two unaffected spouses as technical-artifact controls. Following best-practice guidelines, we performed joint variant calling, including an additional 135 European 1000Genome exomes as a set of background controls. Figure 1 Figure 1. After variant quality control, a total of 676,137 sequence variants were identified. We also performed individual genotype quality control based on a minimum read depth of 10 and genotype quality of 40, resulting in 554,690 variants. For our initial prioritization, we required that variants be: absent in the spouse controls, have minor allele frequency (MAF) ≤ 0.05 in the 1000Genome exomes, and be shared by all four B-cell NHL cases. This resulted in 73 variants of potential interest. Of the 73 variants, seven were predicted to be damaging by either PROVEAN or SIFT, two by both algorithms and by PolyPhen2. These two potentially damaging variants reside in the genes CCDC144A and RRS1. The gene CCDC144A is located at chromosome 17p11.2, a known breakpoint region of the 17p deletion often seen in CLL tumor cells. The variant identified in this gene was rare (MAF = 0.001 in the NHLBI Exome Sequencing Project [ESP]) and was also seen in two additional family members (one with rheumatoid arthritis; a second with rheumatoid arthritis and melanoma). The gene RRS1 is located at chromosome 8q13.1, and has been shown to be important for proper chromosomal organization during mitosis. The variant identified in this gene was relatively rare (MAF = 0.041 in ESP) and was seen in the same, two additional family members. Of the remaining five variants predicted damaging by only one algorithm, of interest were two variants in the SGK223 gene on chromosome 8p23.1. SGK223 is a kinase and a component in the BCR-ABL1 signaling network that is present in most chronic myelogenous leukemia cases and a quarter of adult acute lymphoblastic leukemia cases. Both of the variants in SGK223 were also seen in three additional family members (one with rheumatoid arthritis; a second with rheumatoid arthritis and melanoma; a third with melanoma). In addition to prioritization by predicted function of coding variants, we explored the 73 variants for overlap with findings from published germ-line investigations of B-cell NHL. This identified one variant in the ACOXL gene at chromosome 2q13. The variant is relatively rare (MAF = 0.017 in dbSNP) and lies in the same gene and intron (17,016 base pairs upstream) as rs13401811, the associated SNP (p = 2.08 x 10-18) reported in a genomewide association study (GWAS) for CLL. Our ongoing analyses and prioritization of the variants in this extraordinary family reveal overlap with signals coming from GWAS studies and suggest some potentially damaging variants in genes not previously implicated in NHL. The potential risk-alleles identified in our preliminary findings could shed new light about the genes and genetic factors involved in NHL. Disclosures No relevant conflicts of interest to declare.
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Rodrigues, Gisele O. L., Wenqing Li, Sarah Cramer, Livia W. Campos, Priscila P. Zenatti, Angelo A. B. A. Laranjeira, Julie A. Hixon, et al. "Identification of Genetic Alterations Associated with Mutant IL7Ralpha in T-ALL." Blood 128, no. 22 (December 2, 2016): 5272. http://dx.doi.org/10.1182/blood.v128.22.5272.5272.

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Abstract The IL7/IL7R mediated signaling is essential for normal development and homeostasis of T cell precursors. Early studies have shown that around 10% of patients with Acute lymphoblastic leukemia T cell (T-ALL) have mutations in the alpha chain of the receptor for IL7 (IL-7Ralpha) driving constitutive signaling via JAK1 and independent of IL-7, gamma-chain or JAK3. Some genetic changes are important factors to initiate leukemia, but in many cases these changes are insufficient to achieve the complete leukemic phenotype, suggesting that collaborative oncogenic mutations may be present. To identify candidate mutations that work in collaboration with the oncogenic IL7R, we performed exome sequencing and SNP-CNV-Array assay on a group of eight primary T-ALL samples carrying the IL7R mutation (T-ALL-IL7Rmut). The microarray was performed using Cytoscan HD - Affymetrix and CNVs were detected by ChAs software, version 2.0.1.2. For exome sequencing we used Illumina Hiseq2000 platform and Agilent SureSelect V4 51M Capture kit (mean sequencing depths of 80X / 50X for leukemia and remission samples, respectively). Somatic Single Nucleotide Variants (SNVs) and Small Insertion/Deletion (InDels) were detected using VarScan, and mutations were functionally annotated using ANNOVAR. All somatic mutations detected were manually curated. We found 17 genes recurrently mutated (in ≥ 2 cases) and chose five of them for further analyses due to their previous involvement in ALL (PHF6, RB1, CTCF, SGK223 and DNM2). Ongoing experiments are being conducted to determine whether these recurrent mutations can collaborate functionally with mutIL7R by co-transfection into immature murine thymocytes, transplanting into mice and determining incidence of leukemia. Disclosures No relevant conflicts of interest to declare.
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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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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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Kim, Jeongeun, Donghee Kim, Hyunho Jung, Jinho Lee, and Victor Sukbong Hong. "Identification and Kinetic Characterization of Serum- and Glucocorticoid-Regulated Kinase Inhibitors Using a Fluorescence Polarization–Based Assay." SLAS DISCOVERY: Advancing the Science of Drug Discovery 26, no. 5 (March 30, 2021): 655–62. http://dx.doi.org/10.1177/24725552211002465.

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The serum- and glucocorticoid-regulated kinase (SGK) family consists of three isoforms (SGK1, SGK2, and SGK3) that have been implicated in the regulation of tumor growth, metastasis, autophagy, and epithelial ion transport. SGK1 and SGK3 play essential roles in protein kinase B (AKT or PKB)-independent phosphoinositide 3-kinases (PI3K)-mediated tumorigenesis, as evidenced by the significantly elevated expression levels of SGK1 and SGK3 in many cancers, including prostate cancer, colorectal carcinoma, estrogen-dependent breast cancer, and glioblastoma. Therefore, SGK is a potential target for anticancer therapy. A small kinase-focused library comprising 160 compounds was screened against SGK1 using a fluorescence polarization–based kinase assay that yielded a Z’-factor of 0.82. Among the 39 compounds obtained as initial hits in a primary screen, 12 compounds contained the thiazolidine-2,4-dione scaffold. The inhibitory mechanisms of the most potent hit, KMU010402, were further investigated using kinetic analyses, followed by determination of the inhibition constants for SGK1, SGK2, and SGK3. Molecular modeling was used to propose a potential binding mode of KMU010402 to SGK1.
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Bilanges, Benoit, and Bart Vanhaesebroeck. "Cinderella finds her shoe: the first Vps34 inhibitor uncovers a new PI3K–AGC protein kinase connection." Biochemical Journal 464, no. 2 (November 14, 2014): e7-e10. http://dx.doi.org/10.1042/bj20141218.

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Class II/III PI3Ks (phosphoinositide 3-kinases) produce the PtdIns(3)P lipid that is involved in intracellular vesicular trafficking. In contrast with class I PI3Ks, the potential signalling roles of class II/III PI3Ks are poorly understood. In a recent article in the Biochemical Journal, Bago and co-workers report that Vps34 (vacuolar protein sorting 34), the only class III PI3K, controls the activity of SGK3 (serum- and glucocorticoid-regulated protein kinase 3). Like other AGC kinases, the SGKs (SGK1, SGK2 and SGK3) are activated by dual phosphorylation. Unlike its cousins SGK1 and SGK2, SGK3 contains a PtdIns(3)P-binding domain, providing an additional element of regulation. The study by Bago et al. characterizes and makes extensive use of a Novartis Vps34 inhibitor (VPS34-IN1) that inhibits this PI3K isoform with nanomolar potency, without affecting other lipid kinases or more than 300 protein kinases. The authors show that this compound very rapidly reduced PtdIns(3)P levels at the endosome with concomitant loss of SGK3 phosphorylation. Co-inhibition of class I PI3Ks led to a further reduction in SGK3 activity, indicating that class I PI3Ks may also regulate SGK3 activity through an additional, currently unknown, mechanism. It remains to be assessed whether the novel PI3K–protein kinase connection established by this study is subject to acute cellular stimulation or is part of a constitutive housekeeping function. VPS34-IN1 will provide a useful tool to decipher the kinase-dependent functions of Vps34, with acute changes in SGK3 phosphorylation and subcellular localization being new biomarkers of Vps34 activity.
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Pao, Alan C., James A. McCormick, Hongyan Li, John Siu, Cedric Govaerts, Vivek Bhalla, Rama Soundararajan, and David Pearce. "NH2 terminus of serum and glucocorticoid-regulated kinase 1 binds to phosphoinositides and is essential for isoform-specific physiological functions." American Journal of Physiology-Renal Physiology 292, no. 6 (June 2007): F1741—F1750. http://dx.doi.org/10.1152/ajprenal.00027.2007.

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Serum and glucocorticoid regulated kinase 1 (SGK1) has been identified as a key regulatory protein that controls a diverse set of cellular processes including sodium (Na+) homeostasis, osmoregulation, cell survival, and cell proliferation. Two other SGK isoforms, SGK2 and SGK3, have been identified, which differ most markedly from SGK1 in their NH2-terminal domains. We found that SGK1 and SGK3 are potent stimulators of epithelial Na+ channel (ENaC)-dependent Na+ transport, while SGK2, which has a short NH2 terminus, is a weak stimulator of ENaC. Further characterization of the role of the SGK1 NH2 terminus revealed that its deletion does not affect in vitro kinase activity but profoundly limits the ability of SGK1 either to stimulate ENaC-dependent Na+ transport or inhibit Forkhead-dependent gene transcription. The NH2 terminus of SGK1, which shares sequence homology with the phosphoinositide 3-phosphate [PI( 3 )P] binding domain of SGK3, binds phosphoinositides in protein lipid overlay assays, interacting specifically with PI( 3 )P, PI( 4 )P, and PI( 5 )P, but not with PI( 3 , 4 , 5 )P3. Moreover, a point mutation that reduces phosphoinositide binding to the NH2 terminus also reduces SGK1 effects on Na+ transport and Forkhead activity. These data suggest that the NH2 terminus, although not required for PI 3-kinase-dependent modulation of SGK1 catalytic activity, is required for multiple SGK1 functions, including stimulation of ENaC and inhibition of the proapoptotic Forkhead transcription factor. Together, these observations support the idea that the NH2-terminal domain acts downstream of PI 3-kinase-dependent activation to target the kinase to specific cellular compartments and/or substrates, possibly through its interactions with a subset of phosphoinositides.
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Dissertations / Theses on the topic "SgK223"

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Grothus, Katrin [Verfasser], and Jürgen [Akademischer Betreuer] Daut. "The serine/threonine protein kinase SGK3 stimulates endosomal recycling of the potassium channel Kir2.2. / Katrin Grothus. Betreuer: Jürgen Daut." Marburg : Philipps-Universität Marburg, 2016. http://d-nb.info/109959426X/34.

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Gasser, Jessica Ann. "Serum and Glucocorticoid-Regulated Kinase Signaling in Breast Cancer." Thesis, Harvard University, 2013. http://dissertations.umi.com/gsas.harvard:11296.

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Oncogenic activating mutations in PIK3CA, the gene encoding the catalytic subunit of phosphoinositide 3-kinase (PI 3-K), are highly prevalent in breast cancer. The protein kinase Akt is considered to be the primary effector of PIK3CA, though the mechanisms by which PI 3-K mediates tumorigenic signals in an Akt-independent manner remain obscure. My studies show that the serum and glucocorticoid-regulated kinases (SGKs) can function as effectors of PI 3-kinase and transduce signals to phenotypes associated with malignancy. We show that SGK3 is amplified in breast cancer and identify the mechanism by which SGK3 is activated downstream of PIK3CA, specifically through the catalytic activity of the phosphoinositide phosphatase INPP4B. Expression of INPP4B promotes SGK3 activation and in turn inhibits Akt phosphorylation. In breast cancer cell lines with elevated levels of INPP4B, SGK3 is required for proliferation in 3D and also for invasive migration. SGK3 phenotypes are in part mediated by phosphorylation of the substrate protein N-myc downstream regulated 1 (NDRG1), an established metastasis suppressor. The phosphorylation of NDRG1 leads to recruitment by F-box and WD repeat domain-containing 7 (FBW7), the substrate recognition domain of the Skp, Cullin, F-box containing (SCF) complex. Binding of Fbw7 to NDRG1 promotes its polyubiquitination and subsequent degradation by the 26S proteasome. By contrast, our studies also show that the related SGK1 isoform is polyubiquitinated by the functional E3 ubiquitin ligase Rictor-Cullin-1 complex, leading to SGK1 degradation. Proteasomal degradation of SGK1 by Rictor-Cullin-1is the first identified mTORC2-independent function of the Rictor protein. Moreover, the deregulation of SGK1 ubiquitination highlights a mechanism of SGK1 overexpression in breast cancers.
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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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Lamothe, SHAWN. "The Serum-­‐ and Glucocorticoid-­‐Inducible Kinase SGK1 and SGK3 Regulate hERG Channel Expression via Ubiquitin Ligase Nedd4-­‐2 and GTPase Rab11." Thesis, 2013. http://hdl.handle.net/1974/8169.

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The  rapidly  activating  delayed  rectifier  potassium   channel  (IKr)  encoded  by  the  human  ether-­a-­go-­go  related  gene  (hERG)  is  a  crucial   component  of cardiac  repolarization  of  the  action  potential.  The   gating  kinetics  of  the  channel  and  the  number  of  channels  on  the  membrane  determine  the   degree  of  current  flowing  through  hERG  channels.  Membrane  channel  density  is  directly   related  to  a  balance  between  protein  trafficking  and  degradation.  While  hERG  channel   trafficking  has  been  studied  in  the  past  decade,  recently  our  lab  and  others  have  made  new   discoveries  regarding  hERG  degradation.  These  studies  show  that  Neural  Down  Regulated   Gene  4  subtype  2  (Nedd4-­‐2)  is  the  ligase  that  covalently  attaches  ubiquitin  to  the  hERG   channel  and  facilitates  degradation  (Albesa  et  al.,  2011;Guo  et  al.,  2012).  Given  these   findings,  my  goal/objective  was  to  study  the  molecular  mechanisms  that  control  the   destructive  effects  of  Nedd4-­‐2  on  the  hERG  channel.  In  the  present  study,  I  demonstrated   that  overexpression  of  the  stress-­‐responsive  serum-­‐  and  glucocorticoid-­‐inducible  kinase   (SGK)  isoforms  SGK1  and  SGK3  increase  the  current  and  expression  level  of  the  membrane-­‐ localized  mature  proteins  of  hERG  channels  stably  expressed  in  HEK  293  (hERG-­‐HEK)  cells.   I  have  found  that  the  overexpression  of  SGK1  and  SGK3  increased  Nedd4-­‐2   phosphorylation,  which  is  known  to  inhibit  Nedd4-­‐2  activity.  Furthermore,  the  synthetic   glucocorticoid,  dexamethasone,  increased  the  current  and  abundance  of  mature  ERG   proteins  in  both  hERG-­‐HEK  cells  and  neonatal  rat  cardiac  myocytes  through  the   enhancement  of  SGK1  but  not  SGK3  expression.  Additionally,  disruption  of  Rab11  proteins led  to  a  complete  elimination  of  SGK-­‐mediated  increase  in  hERG  expression.  These  results   indicate  that  SGK  enhances  the  expression  level  of  mature  hERG  channels  by  inhibiting   Nedd4-­‐2  as  well  as  by  promoting  Rab11-­‐mediated  hERG  recycling.
Thesis (Master, Physiology) -- Queen's University, 2013-08-14 16:01:43.951
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Conference papers on the topic "SgK223"

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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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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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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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Jiang, Chen Chen, Meng Na Chi, Su Tang Guo, James S. Wilmott, Xiang Yun Guo, Xu Guang Yan, Chun Yan Wang, et al. "Abstract 4718: Inositol polyphosphate 4-phosphatase II activates PI3K/SGK3 signaling to promote proliferation of human melanoma cells." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4718.

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Liu, Dan, and Bhuvanesh Dave. "Abstract 3441: A RPL39-SGK3 signaling pathway that may play a key role in breast cancer therapy resistance." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-3441.

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Liu, Dan, and Bhuvanesh Dave. "Abstract 3441: A RPL39-SGK3 signaling pathway that may play a key role in breast cancer therapy resistance." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-3441.

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Bago, Ruzica, Eeva Sommer, Nazma Malik, Michael J. Munson, Alan R. Prescott, Paul Davies, Shpiro Natalia, Ian G. Ganley, and Dario R. Alessi. "Abstract A04: Characterization of VPS34-IN1, a specific inhibitor of Vps34 reveals that the phosphatidylinositol 3-phosphate binding SGK3 protein kinase is regulated by class III PI-3 kinase." In Abstracts: AACR Special Conference: Targeting the PI3K-mTOR Network in Cancer; September 14-17, 2014; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-8514.pi3k14-a04.

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