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Regulated Protein Degradation

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 Degradation

Regulated Protein Degradation

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

The Proteasome

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Translocation of Proteins into the Mitochondria

Translocation of Proteins into the Mitochondria

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Covalently Linked Protein Regulators

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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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Related Experiment Video

Updated: Apr 14, 2026

Time-Lapse Video Microscopy for Assessment of EYFP-Parkin Aggregation as a Marker for Cellular Mitophagy

Time-Lapse Video Microscopy for Assessment of EYFP-Parkin Aggregation as a Marker for Cellular Mitophagy

Published on: May 4, 2016

Deubiquitinating enzymes regulate PARK2-mediated mitophagy.

Yuqing Wang¹, Mauro Serricchio, Miluska Jauregui

¹a Cell Biology Program ; The Hospital for Sick Children ; Toronto , ON Canada.

|April 28, 2015

Summary

Mitochondrial deubiquitinating enzymes USP30 and USP35 regulate mitophagy, a key process for cellular health. These enzymes can delay mitophagy, offering potential therapeutic targets for neurodegenerative diseases.

Keywords:

CCCP Cer, cerulean DMSO, dimethyl sulfoxide DUB DsRed, Discosoma sp. red fluorescent protein GAPDH, glyceraldehyde 3-phosphate dehydrogenase GFP, green fluorescent protein HA, human influenza hemagglutinin MFN2, mitofusin 2 MTS OMM, outer mitochondrial membrane PARK2 PARK2, parkin RBR E3 ubiquitin protein ligase PINK1, PTEN-induced putative kinase 1 SYNJ2BP, synaptojanin 2 binding protein TOMM20, translocase of outer mitochondrial membrane 20 homolog (yeast)USP, ubiquitin specific peptidase USP30 USP35 autophagy carbonyl cyanide m-chlorophenylhydrazone deubiquitinating enzyme deubiquitinating enzymes l-USP35, long form of ubiquitin specific peptidase 35 mitochondrial dynamics mitochondrial targeting sequence mitophagy neurodegenerative diseases s-USP35, short form of ubiquitin specific peptidase 35 ubiquitin

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Screening Traditional Chinese Medicine Compounds for Inhibiting UCHL3 Activity Based on Molecular Docking and Deubiquitinating Enzyme Probe Technology

Screening Traditional Chinese Medicine Compounds for Inhibiting UCHL3 Activity Based on Molecular Docking and Deubiquitinating Enzyme Probe Technology

Published on: November 22, 2024

Area of Science:

Cell Biology
Molecular Biology
Neuroscience

Background:

Mitophagy is crucial for mitochondrial quality control, primarily mediated by PINK1 and PARK2/Parkin.
Ubiquitination of mitochondrial proteins is central to mitophagy, but the role of deubiquitinating enzymes (DUBs) remains largely unknown.

Purpose of the Study:

To investigate the role of mitochondrial DUBs, specifically USP30 and USP35, in regulating PARK2/Parkin-mediated mitophagy.
To elucidate the mechanisms by which USP30 and USP35 influence mitophagy and PARK2 recruitment.

Main Methods:

Quantitative mitophagy assays were employed to measure the rate of mitophagy.
Mitochondrial localization and translocation of USP30 and USP35 were analyzed during mitophagy induction.

Main Results:

USP30 and USP35 were found to delay PARK2/Parkin-mediated mitophagy.
USP30 delays mitophagy by inhibiting PARK2 recruitment to mitochondria.
USP35 regulates mitophagy via a mechanism independent of PARK2 recruitment, associating with polarized mitochondria and translocating to the cytosol.

Conclusions:

Mitochondrial-associated DUBs, USP30 and USP35, play significant regulatory roles in mitophagy.
These findings highlight potential therapeutic targets for neurodegenerative diseases linked to mitochondrial dysfunction.