Related Researcher

Author's Photo

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


TAZ Suppresses NFAT5 Activity through Tyrosine Phosphorylation

DC Field Value Language Jang, Eun Jung ko Jeong, Hana ko Han, Ki Hwan ko Kwon, H. Moo ko Hong, Jeong-Ho ko Hwang, Eun Sook ko 2014-04-09T08:35:18Z - 2013-06-07 ko 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 -
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.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 * 2015-02-28 * 2014-07-12 *
dc.identifier.doi 10.1128/MCB.00392-12 ko
dc.identifier.url ko
Appears in Collections:
BIO_Journal Papers

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show simple item record


  • mendeley


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.