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Related Concept Videos

Delivery Pathways to the Lysosome01:36

Delivery Pathways to the Lysosome

Eukaryotic cells use different mechanisms to eliminate toxic waste obsolete and worn-out substances. Lysosomes play a pivotal role in this, and hence, these substances are carried to the lysosome from other parts of the cell and extracellular space through different pathways. The most elaborately studied pathways to the lysosome are the endocytic pathways.
Endocytosis
In endocytosis, the cell membrane takes up macromolecules and particles from the surrounding medium. Clathrin-mediated...
Autophagy01:27

Autophagy

Autophagy is a self-digesting process by which a cell protects itself from threats both within and outside the cell, ranging from abnormal proteins to invading bacteria. In this process, obsolete components of the cell and invading microbes are degraded by hydrolytic enzymes active in an acidic environment of the lysosomal lumen.
An autophagic pathway consists of a series of signaling events activated in response to diverse stress and physiological conditions such as food deprivation,...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
These groups modify specific amino acids in a protein.
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Phosphorylation01:02

Phosphorylation

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.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

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Related Experiment Video

Updated: May 21, 2026

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells
09:10

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells

Published on: October 28, 2019

Lysine modifications and autophagy.

Kristi L Norris1, Tso-Pang Yao

  • 1Department of Pharmacology and Cancer Biology, Duke University, Durham, NC 27710, U.S.A.

Essays in Biochemistry
|June 20, 2012
PubMed
Summary
This summary is machine-generated.

Autophagy, a cellular process vital for metabolism and immunity, is regulated by post-translational modifications (PTMs). Acetylation and ubiquitination of key proteins critically impact autophagy, offering potential therapeutic targets for diseases like cancer.

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A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Related Experiment Videos

Last Updated: May 21, 2026

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells
09:10

siRNA Electroporation to Modulate Autophagy in Herpes Simplex Virus Type 1-Infected Monocyte-Derived Dendritic Cells

Published on: October 28, 2019

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Autophagy is a conserved catabolic pathway crucial for cellular adaptation to stress and nutrient deprivation.
  • This process is essential for metabolism, immunity, and development, and its dysregulation is implicated in diseases like cancer and neurodegeneration.
  • Understanding autophagy regulation is critical for both basic science and clinical applications.

Purpose of the Study:

  • To explore how post-translational modifications (PTMs) of lysine residues, specifically acetylation and ubiquitination, influence autophagy.
  • To examine the role of these PTMs in the activation, maturation, and substrate selectivity of the autophagy pathway.
  • To discuss the therapeutic potential of targeting these PTMs for modulating autophagic activity.

Main Methods:

  • Review and discussion of existing literature on PTMs in autophagy.
  • Analysis of how acetylation and ubiquitination affect key autophagy-related proteins.
  • Exploration of the functional consequences of these modifications on autophagic processes.

Main Results:

  • Post-translational modifications, including acetylation and ubiquitination, significantly alter the function of proteins central to autophagy.
  • These modifications impact critical steps such as the initiation, elongation, and cargo recognition of autophagosomes.
  • Specific lysine residues are identified as key sites for regulatory modifications.

Conclusions:

  • PTMs, particularly acetylation and ubiquitination, are crucial regulators of autophagy.
  • Targeting these specific protein modifications presents a promising strategy for therapeutic intervention in autophagy-related diseases.
  • Further research into PTMs will enhance our understanding and manipulation of autophagy.