AI Article Synopsis
- Pin1 is an enzyme that catalyzes the isomerization of specific peptide bonds, impacting various biological processes, including the formation of fat cells (adipogenesis).
- Research shows that when Pin1 is overexpressed in certain cell types, it promotes the differentiation of fat cells, while inhibiting Pin1 has the opposite effect.
- The study identifies that Pin1 interacts with PPARγ, a crucial protein for fat cell development, and suggests that this interaction, including the involvement of ERK activity, is vital for enhancing adipocyte differentiation.
Article 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.
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| http://dx.doi.org/10.1016/j.mce.2016.07.030 | DOI Listing |
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