Pin1 enhances adipocyte differentiation by positively regulating the transcriptional activity of PPARγ

Younho Han, Sung Ho Lee, Minjin Bahn, Chang Yeol Yeo, Kwang Youl Lee

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

Abstract

Pin1 is a peptidylprolyl cis/trans isomerase and it has a unique enzymatic activity of catalyzing isomerization of the peptide bond between phospho-serine/threonine and proline. Through the conformational change of its substrates, Pin1 regulates diverse biological processes including adipogenesis. In mouse embryonic fibroblasts and 3T3-L1 preadipocytes, overexpression of Pin1 enhances adipocyte differentiation whereas inhibition of Pin1 activity suppresses it. However, the precise functions of Pin1 during adipogenesis are not clear. In the present study, we investigated the potential targets of Pin1 during adipogenesis. We found that Pin1 interacts directly with and regulates the transcriptional activity of PPARγ, a key regulator of adipogenesis. In addition, ERK activity and Ser273 of PPARγ, a potential ERK phosphorylation target site, are important for the regulation of PPARγ function by Pin1 in 3T3-L1 cells. Taken together our results suggest a novel regulatory mechanism of Pin1 during adipogenesis, in which Pin1 enhances adipocyte differentiation by regulating the function of PPARγ.

Original languageEnglish
Pages (from-to)150-158
Number of pages9
JournalMolecular and Cellular Endocrinology
Volume436
DOIs
StatePublished - 15 Nov 2016

Keywords

  • Adipogenesis
  • ERK
  • Pin1
  • PPARγ

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