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Kwon, Hyug Moo
Immunometabolism and Cancer Lab
Research Interests
  • TonEBP, Obesity, Cancer, Chronic inflammatory diseases, Brain disorder, Kidney disorder, Genomic instability

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TAZ Suppresses NFAT5 Activity through Tyrosine Phosphorylation

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dc.contributor.author Jang, Eun Jung ko
dc.contributor.author Jeong, Hana ko
dc.contributor.author Han, Ki Hwan ko
dc.contributor.author Kwon, H. Moo ko
dc.contributor.author Hong, Jeong-Ho ko
dc.contributor.author Hwang, Eun Sook ko
dc.date.available 2014-04-09T08:35:18Z -
dc.date.created 2013-06-07 ko
dc.date.issued 2012-12 ko
dc.identifier.citation MOLECULAR AND CELLULAR BIOLOGY, v.32, no.24, pp.4925 - 4932 ko
dc.identifier.issn 0270-7306 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/2712 -
dc.description.abstract Transcriptional coactivator with PDZ-binding motif (TAZ) physically interacts with a variety of transcription factors and modulates their activities involved in cell proliferation and mesenchymal stem cell differentiation. TAZ is highly expressed in the kidney, and a deficiency of this protein results in multiple renal cysts and urinary concentration defects; however, the molecular functions of TAZ in renal cells remain largely unknown. In this study, we examined the effects of osmotic stress on TAZ expression and activity in renal cells. We found that hyperosmotic stress selectively increased protein phosphorylation at tyrosine 316 of TAZ and that this was enhanced by c-Abl activation in response to hyperosmotic stress. Interestingly, phosphorylated TAZ physically interacted with nuclear factor of activated T cells 5 (NFAT5), a major osmoregulatory transcription factor, and subsequently suppressed DNA binding and transcriptional activity of NFAT5. Furthermore, TAZ deficiency elicited an increase in NFAT5 activity in vitro and in vivo, which then reverted to basal levels following restoration of wild-type TAZ but not mutant TAZ (Y316F). Collectively, the data suggest that TAZ modulates cellular responses to hyperosmotic stress through fine-tuning of NFAT5 activity via tyrosine phosphorylation. ko
dc.description.statementofresponsibility open -
dc.language 영어 ko
dc.publisher AMER SOC MICROBIOLOGY ko
dc.title TAZ Suppresses NFAT5 Activity through Tyrosine Phosphorylation ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-84871860525 ko
dc.identifier.wosid 000311492200004 ko
dc.type.rims ART ko
dc.description.wostc 3 *
dc.description.scopustc 3 *
dc.date.tcdate 2015-02-28 *
dc.date.scptcdate 2014-07-12 *
dc.identifier.doi 10.1128/MCB.00392-12 ko
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=84871860525 ko
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