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Related Experiment Video

Updated: May 11, 2026

An Adipocyte Cell Culture Model to Study the Impact of Protein and Micro-RNA Modulation on Adipocyte Function

An Adipocyte Cell Culture Model to Study the Impact of Protein and Micro-RNA Modulation on Adipocyte Function

Published on: May 4, 2021

Lipin1 regulates PPARγ transcriptional activity.

Hee Eun Kim¹, Eunju Bae, Deok-Yoon Jeong

¹Department of Biochemistry and Molecular Biology, Brain Korea 21 Project for Medical Science, Institute of Genetic Science, Integrated Genomic Research Center for Metabolic Regulation, Yonsei University College of Medicine, Seoul 120-752, Korea.

The Biochemical Journal

|May 1, 2013

Summary

Lipin1 activates peroxisome-proliferator-activated receptor γ (PPARγ) by releasing co-repressors, enhancing adipocyte differentiation. A novel transcriptional activation domain and VXXLL motif in lipin1 are crucial for this PPARγ regulation.

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Last Updated: May 11, 2026

An Adipocyte Cell Culture Model to Study the Impact of Protein and Micro-RNA Modulation on Adipocyte Function

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Published on: May 4, 2021

Isolation and Differentiation of Adipose-Derived Stem Cells from Porcine Subcutaneous Adipose Tissues

Isolation and Differentiation of Adipose-Derived Stem Cells from Porcine Subcutaneous Adipose Tissues

Published on: March 31, 2016

Area of Science:

Molecular Biology
Cell Biology
Biochemistry

Background:

Peroxisome-proliferator-activated receptor γ (PPARγ) is a key transcription factor regulating adipogenesis.
Lipin1 modulates the PPARγ network, but its mechanism of action on PPARγ activity is unclear.

Purpose of the Study:

To elucidate the mechanism by which lipin1 affects the transcriptional activity of PPARγ.
To identify specific regions and motifs in lipin1 responsible for PPARγ regulation.

Main Methods:

Co-immunoprecipitation assays to detect physical interactions.
Reporter gene assays to assess transcriptional activity.
Site-directed mutagenesis to identify critical functional domains and motifs.

Main Results:

Lipin1 activates PPARγ by releasing co-repressors (NCoR1, SMRT) independently of rosiglitazone.
A novel lipin1 transcriptional activation domain (TAD) between residues 217-399 is critical for PPARγ activation.
The C-terminal region (residues 825-926) and a VXXLL motif at residue 885 in lipin1 are essential for PPARγ binding and activation.
Lipin1 enhances adipocyte differentiation via its TAD and VXXLL motif, without direct involvement of its catalytic activity.

Conclusions:

Lipin1 acts as a crucial co-activator of PPARγ, promoting adipocyte differentiation.
Lipin1's co-activation mechanism involves releasing co-repressors and utilizing a specific TAD and VXXLL motif.
This regulatory role of lipin1 on PPARγ is distinct from its effects on PPARα activation.