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STK38 is a PPARγ-interacting protein promoting adipogenesis.
Kun Qian1,2, Daozhan Yu2, Weiming Wang2
1Department of Gastrointestinal Surgery, The First Affiliated Hospital of Chongqing Medical University, Chongqing, China.
Adipocyte
|October 21, 2021
Summary
Serine/threonine kinase 38 (STK38) stabilizes Peroxisome proliferator-activated receptor-γ (PPARγ), enhancing its activity. This STK38-PPARγ interaction promotes adipogenesis, revealing a novel cofactor role in fat cell formation.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Peroxisome proliferator-activated receptor-γ (PPARγ) is crucial for adipogenesis.
- Regulation of PPARγ at the protein level remains poorly understood.
Purpose of the Study:
- To identify proteins interacting with PPARγ that modulate its protein levels and activity in human adipocytes.
- To elucidate the role of identified interacting proteins in adipogenesis.
Main Methods:
- Flag-tagged PPARγ expressed in human preadipocytes as bait.
- Mass spectrometry and proteomics for protein identification.
- Protein pulldown, reporter assays, and cell-based assays to confirm interactions and function.
Main Results:
- Serine/threonine kinase 38 (STK38) identified as a major PPARγ-interacting protein.
- STK38 enhances PPARγ transactivating activity and increases PPARγ protein stability (half-life extended from ~1.08 to 1.95 h).
- STK38 overexpression promotes adipogenesis, while knockdown impairs it in a PPARγ-dependent manner.
Conclusions:
- STK38 is a novel cofactor that promotes adipogenesis.
- STK38 likely stabilizes PPARγ, thereby enhancing its function in fat cell differentiation.
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