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Related Concept Videos

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.
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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...
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...
The Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
The Proteasome01:13

The Proteasome

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Related Experiment Video

Updated: Jul 6, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Prolyl hydroxylase PHD3 activates oxygen-dependent protein aggregation.

Krista Rantanen1, Juha Pursiheimo, Heidi Högel

  • 1Turku Centre for Biotechnology, Turku University and Abo Akademi University, FIN-29521 Turku, Finland.

Molecular Biology of the Cell
|March 14, 2008
PubMed
Summary

The cellular oxygen sensor PHD3 forms aggresome-like aggregates under normal oxygen conditions, which precedes apoptosis. Hypoxia or inhibited activity reduces this aggregation, revealing PHD3

More Related Videos

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Related Experiment Videos

Last Updated: Jul 6, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • HIF prolyl hydroxylases (PHDs/EGLNs) regulate cellular responses to oxygen levels.
  • PHD3, a specific isoform, is induced by hypoxia and promotes apoptosis in oxygenated neural cells.

Purpose of the Study:

  • To investigate the oxygen-dependent subcellular aggregation of PHD3.
  • To determine the relationship between PHD3 aggregation, proteasomal function, and apoptosis.

Main Methods:

  • Microscopy to observe PHD3 aggregation under varying oxygen conditions.
  • Biochemical assays to analyze aggregate composition (proteasome, chaperones, ubiquitin).
  • Cellular assays in HeLa cells to assess apoptosis induction and proteasomal aggregation.

Main Results:

  • PHD3 forms aggresome-like structures in an oxygen-dependent manner, primarily under normoxia.
  • Aggregation is reduced by hypoxia or inactivation of PHD3 hydroxylase activity.
  • PHD3 aggregates contain proteasomal components and depend on microtubular integrity.
  • Forced expression of active PHD3 induces proteasomal aggregation and apoptosis in HeLa cells.

Conclusions:

  • PHD3 acts as a cellular oxygen sensor that regulates protein aggregation.
  • PHD3-mediated aggregation is linked to apoptosis under normoxic conditions.
  • This study reveals a novel role for PHD3 in cellular protein quality control and stress response.