(-)-Epigallocatechin-3-gallate stimulates myogenic differentiation through TAZ activation.
Muscle loss is a typical process of aging. Green tea consumption is known to slow down the progress of aging. Their underlying mechanisms, however, remain largely unknown. In this study, we investigated the effect of (-)-epigallocatechin-3-gallate (EGCG), a polyphenolic compound of green tea, on myogenic differentiation and found that EGCG significantly increases myogenic differentiation. After EGCG treatment, the expression of myogenic marker genes, such as myosin heavy chain, are increased through activation of TAZ, a transcriptional coactivator with a PDZ-binding motif. TAZ-knockdown does not stimulate EGCG-induced myogenic differentiation. EGCG facilitates the interaction between TAZ and MyoD, which stimulates MyoD-mediated gene transcription. EGCG induces nuclear localization of TAZ through the dephosphorylation of TAZ at its Ser89 residue, which relieves 14-3-3 binding in the cytosol. Interestingly, inactivation of Lats kinase is observed after EGCG treatment, which is responsible for the production of dephosphorylated TAZ. Together, these results suggest that EGCG induces myogenic differentiation through TAZ, suggesting that TAZ plays an important role in EGCG induced muscle regeneration.
Department of Life Sciences, School of Life Sciences and Biotechnology, Korea University, Seoul 02841, South Korea.
A Rum
AR
Kim
Department of Life Sciences, School of Life Sciences and Biotechnology, Korea University, Seoul 02841, South Korea.
Kyung Min
KM
Kim
Department of Life Sciences, School of Life Sciences and Biotechnology, Korea University, Seoul 02841, South Korea.
Mi Ran
MR
Byun
Department of Life Sciences, School of Life Sciences and Biotechnology, Korea University, Seoul 02841, South Korea.
Jun-Ha
JH
Hwang
Department of Life Sciences, School of Life Sciences and Biotechnology, Korea University, Seoul 02841, South Korea.
Jung Il
JI
Park
Department of Life Sciences, School of Life Sciences and Biotechnology, Korea University, Seoul 02841, South Korea.
Ho Taek
HT
Oh
College of Pharmacy, Ewha Woman's University, Seoul 03760, South Korea.
Mi Gyeong
MG
Jeong
College of Pharmacy, Ewha Woman's University, Seoul 03760, South Korea. Electronic address: eshwang@ewha.ac.kr.
Eun Sook
ES
Hwang
Department of Life Sciences, School of Life Sciences and Biotechnology, Korea University, Seoul 02841, South Korea. Electronic address: jh_hong@korea.ac.kr.
Jeong-Ho
JH
Hong
D048948:14-3-3 Proteins / Q000235:genetics / Q000378:metabolism; D000217:Acyltransferases; D000818:Animals; D002392:Catechin / Q000031:analogs & derivatives* / Q000494:pharmacology; D002454:Cell Differentiation / Q000187:drug effects*; D002460:Cell Line; D005786:Gene Expression Regulation; D057809:HEK293 Cells; D006801:Humans; D051379:Mice; D008810:Mice, Inbred C57BL; D017570:MyoD Protein / Q000235:genetics / Q000378:metabolism; D032446:Myoblasts / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D018008:Myogenin / Q000235:genetics / Q000378:metabolism; D018995:Myosin Heavy Chains / Q000235:genetics / Q000378:metabolism; D061251:Primary Cell Culture; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors / Q000235:genetics / Q000378:metabolism; D032496:Satellite Cells, Skeletal Muscle / Q000166:cytology / Q000187:drug effects* / Q000378:metabolism; D015398:Signal Transduction; D013662:Tea / Q000737:chemistry; D014157:Transcription Factors / Q000819:agonists* / Q000235:genetics / Q000378:metabolism
D048948:14-3-3 Proteins; D017570:MyoD Protein; C057363:MyoD1 myogenic differentiation protein; C503801:Myog protein, mouse; D018008:Myogenin; D013662:Tea; D014157:Transcription Factors; D002392:Catechin; C045651:epigallocatechin gallate; D000217:Acyltransferases; C486363:tafazzin protein, mouse; C108675:TAFAZZIN protein, human; C490501:Lats1 protein, mouse; D017346:Protein Serine-Threonine Kinases; D018995:Myosin Heavy Chains
Catechins; Myogenesis; Satellite cells; TAZ