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Related Concept Videos

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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IP3/DAG Signaling Pathway01:11

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Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and...
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Cell Specific Gene Expression01:58

Cell Specific Gene Expression

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Multicellular organisms contain a variety of structurally and functionally distinct cell types, but the DNA in all the cells originated from the same parent cells. The differences in the cells can be attributed to the differential gene expression. Liver cells, whose functions include detoxification of blood, production of bile to metabolize fats, and synthesis of proteins essential for metabolism, must express a specific set of genes to perform their functions. Gene expression also varies with...
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cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

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Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

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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...
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Lipid Catabolism01:25

Lipid Catabolism

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Triglycerides serve as crucial long-term energy storage molecules in microorganisms, providing a dense source of metabolic energy. Their breakdown is mediated by lipases, which hydrolyze triglycerides into glycerol and free fatty acids. Each of these components follows distinct metabolic pathways, ultimately contributing to ATP synthesis and cellular energy homeostasis.Glycerol MetabolismGlycerol, released from triglyceride hydrolysis, is phosphorylated by glycerol kinase to form...
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  • Physical Sciences
  • Condensed Matter Physics
  • Surface Properties Of Condensed Matter
  • Pi(4)p Recruits Cide Proteins To Promote The Formation Of Unilocular Lipid Droplets During Adipogenesis And Hepatic Steatosis.
  • Physical Sciences
  • Condensed Matter Physics
  • Surface Properties Of Condensed Matter
  • Pi(4)p Recruits Cide Proteins To Promote The Formation Of Unilocular Lipid Droplets During Adipogenesis And Hepatic Steatosis.

    • Related Experiment Video

    Isolation and Differentiation of Adipose-Derived Stem Cells from Porcine Subcutaneous Adipose Tissues
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    PI(4)P recruits CIDE proteins to promote the formation of unilocular lipid droplets during adipogenesis and hepatic steatosis.

    Jin Wu1,2, Mingming Gao2,3, Xiaoqin Wu2,4

    • 1Shanghai Key Laboratory of Metabolic Remodeling and Health, State Key Laboratory of Genetics and Development of Complex Phenotypes, Institute of Metabolism and Integrative Biology, School of Life Sciences, Department of Endocrinology and Metabolism, Zhongshan Hospital, Fudan University, Shanghai 200438, China.

    Proceedings of the National Academy of Sciences of the United States of America
    |July 3, 2025

    View abstract on PubMed

    Summary
    This summary is machine-generated.

    Phosphatidylinositol 4-phosphate (PI(4)P) on lipid droplets recruits CIDE proteins, regulating their size and function. Depleting PI(4)P in adipocytes and steatotic liver reduces lipid droplet size.

    Keywords:
    CIDEPI(4)Padipogenesislipid droplets

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

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

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

    Published on: May 4, 2021

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    Area of Science:

    • Cell Biology
    • Metabolism
    • Lipid Biology

    Background:

    • Lipid droplets (LDs) are crucial metabolic organelles enclosed by a phospholipid monolayer.
    • The specific roles of LD surface phospholipids in LD regulation are not fully understood.
    • Phosphoinositides are key regulators of organelle function.

    Purpose of the Study:

    • To investigate the role of phosphoinositides, specifically PI(4)P, on the surface of lipid droplets.
    • To determine how PI(4)P influences the recruitment and function of CIDE proteins.
    • To elucidate the impact of PI(4)P on LD size and metabolic processes.

    Main Methods:

    • Investigated PI(4)P localization on LDs.
    • Examined the effect of ORP2 and ORP5 expression on CIDE protein localization.
    • Utilized PI4K2A knockdown to block PI(4)P synthesis.
    • Assessed LD size and adipose tissue mass in adipocytes.
    • Analyzed LD enlargement in steatotic liver models.

    Main Results:

    • PI(4)P was identified on a subset of LDs, recruiting and activating CIDE proteins.
    • Enhanced expression of ORP2/ORP5 or PI4K2A knockdown disrupted CIDE protein localization and function.
    • Depletion of PI(4)P in adipocytes significantly reduced LD size and adipose tissue mass.
    • In steatotic liver, PI(4)P depletion impaired LD enlargement.

    Conclusions:

    • LD surface PI(4)P is essential for recruiting and activating CIDE proteins.
    • PI(4)P plays a critical role in regulating lipid droplet size and adipose tissue mass.
    • This study reveals a novel mechanism for CIDE protein recruitment to LDs via PI(4)P.