Related Experiment Video

Updated: Apr 28, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

8.8K

Small ubiquitin-like modifier (SUMO) protein-specific protease 1 de-SUMOylates Sharp-1 protein and controls adipocyte

Bingting Liu1, Tianshi Wang1, Wenhan Mei2

  • 1From the Department of Biochemistry and Molecular Cell Biology, Shanghai Key Laboratory for Tumor Microenvironment and Inflammation and State Key Laboratory of Oncogenes and Related Genes, Shanghai Cancer Institute, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.

The Journal of Biological Chemistry
|June 20, 2014
PubMed

Insights

SENP1 promotes adipocyte differentiation by de-SUMOylating Sharp-1, a repressor of peroxisome proliferator-activated receptor γ (PPARγ). This action enhances PPARγ expression and adipogenesis, identifying SENP1 as a novel regulator in the process.

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Adipocyte differentiation is a complex process regulated by key transcription factors.
  • Peroxisome proliferator-activated receptor γ (PPARγ) is a crucial nuclear receptor in adipogenesis.
  • SUMOylation is a post-translational modification that can regulate protein function and gene expression.

Purpose of the Study:

  • To investigate the role of SENP1 in adipocyte differentiation.
  • To identify the molecular mechanism by which SENP1 regulates adipogenesis.
  • To determine if SENP1 interacts with or modifies known adipogenic regulators.

Main Methods:

  • Utilized Senp1 knockout (Senp1(-/-)) mouse embryonic fibroblast cells.
  • Induced adipogenesis using specific stimuli.
  • Assessed adipocyte differentiation and PPARγ expression.
  • Investigated the de-SUMOylation activity of SENP1 on Sharp-1.

Main Results:

  • Senp1(-/-) cells exhibited defects in adipocyte differentiation and PPARγ expression.
  • SENP1 was identified as a specific de-SUMOylase for Sharp-1.
  • SENP1 de-SUMOylates Sharp-1, releasing its repression on PPARγ transcription.
  • SENP1 enhances adipogenesis by promoting PPARγ expression via Sharp-1 de-SUMOylation.

Conclusions:

  • SENP1 is a novel and essential regulator of adipocyte differentiation.
  • SENP1 enhances adipogenesis through the de-SUMOylation of the PPARγ repressor, Sharp-1.
  • Targeting SENP1 may offer a new therapeutic strategy for metabolic disorders related to adipogenesis.
Keywords:
AdipogenesisCell DifferentiationGene TranscriptionPeroxisome Proliferator-activated Receptor (PPAR)SUMOylation

More Related Videos

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells09:40

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

6.6K
SUMO-Binding Entities SUBEs as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer08:29

SUMO-Binding Entities SUBEs as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

Published on: November 1, 2019

7.5K

Related Concept Videos

The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
10.1K
TGF - β Signaling Pathway01:16

TGF - β Signaling Pathway

The TGF-β signaling pathway regulates cell growth, differentiation, adhesion, motility, and development. TGF-β ligands that induce TGF-β signaling are synthesized in their latent form. Several proteases or cell surface receptors such as integrins act upon the latent form, releasing the active ligand. There are three types of mammalian TGF-βs: (TGF-β1, TGF-β2, and TGF-β3) that bind as homodimers or heterodimers to TGF-β receptors. The TGF-β receptors...
7.1K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
2.5K
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
6.6K
Regulated Protein Degradation02:58

Regulated Protein Degradation

2.4K
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
15.2K