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Lipids as Anchors01:32

Lipids as Anchors

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In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
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Phosphorylation01:02

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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Covalently Linked Protein Regulators02:04

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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Phosphoinositides and PIPs01:42

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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.
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Overview of Lipid Metabolism01:24

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Lipid metabolism is a crucial process in the human body that involves the synthesis and degradation of lipids. This process is essential for energy production, cell membrane formation, and hormone production, among other functions.
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Related Experiment Video

Updated: Dec 4, 2025

Optimized Incorporation of Alkynyl Fatty Acid Analogs for the Detection of Fatty Acylated Proteins using Click Chemistry
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Protein palmitoylation and its pathophysiological relevance.

Jiayu Jin1, Xiuling Zhi1, Xinhong Wang1

  • 1Shanghai Key Laboratory of Bioactive Small Molecules, Department of Physiology and Pathophysiology, Fudan University, Shanghai, China.

Journal of Cellular Physiology
|October 23, 2020
PubMed
Summary

Protein palmitoylation, a key lipid modification, regulates vital cellular functions and protein trafficking. Its dysregulation, often linked to DHHC protein palmitoyl transferases (PATs), contributes to human diseases, highlighting therapeutic potential.

Keywords:
DHHC-PATshuman diseasespalmitoylationposttranslational modificationprotein trafficking

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Protein palmitoylation involves attaching C16 fatty acids to cysteine residues via a reversible thioester bond.
  • This lipid modification is crucial for protein stability, localization, trafficking, and interactions.
  • Palmitoylation is primarily regulated by DHHC family protein palmitoyl transferases (PATs) and is reversible.

Purpose of the Study:

  • To elucidate the fundamental mechanisms of protein palmitoylation.
  • To explore the role of PATs in cellular processes and human diseases.
  • To investigate the interplay of palmitoylation with other posttranslational modifications.

Main Methods:

  • Review of existing literature on protein palmitoylation.
  • Analysis of the role of DHHC PATs in cellular signaling.
  • Examination of disease-associated mutations in PATs.

Main Results:

  • Palmitoylation is a dynamic and reversible process essential for numerous cellular functions.
  • PATs are critical regulators of protein trafficking and stability.
  • Mutations in PATs are implicated in diseases including cancer and neurological disorders.
  • Palmitoylation dynamics are influenced by ubiquitination and phosphorylation.

Conclusions:

  • Understanding protein palmitoylation mechanisms offers insights into disease pathogenesis.
  • The reversibility and regulation of palmitoylation present potential therapeutic targets.
  • Targeting PATs and their regulatory networks may offer novel treatment strategies for various human diseases.