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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

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 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 (ubiquitin...

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst 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. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst 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. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

The Role of Actin and Myosin in Non-muscle Cells

The Role of Actin and Myosin in Non-muscle Cells

Actin and myosin or actomyosin filaments also play a significant role in cells other than those involved in muscle contraction (which occurs within the sarcomere of muscle cells). The mechanism of non-muscle cell contractile bundles was first observed in Dictyostelium and Acanthamoeba. In non-muscle cells, two bundles are commonly found: stress fibers and actomyosin adherence belts. These contractile bundles are smaller and less organized than the ones found in muscle cells. They are held...

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Related Experiment Video

Updated: Jun 21, 2026

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Cycloheximide Chase Analysis of Protein Degradation in Saccharomyces cerevisiae

Published on: April 18, 2016

Cellular contractility requires ubiquitin mediated proteolysis.

Yuval Cinnamon¹, Oren Feine, Helfrid Hochegger

¹The Department of Genetics, The Silberman Institute of Life Sciences, The Hebrew University of Jerusalem, Givat Ram, Jerusalem, Israel.

|July 15, 2009

Summary

Cellular contractility relies on ubiquitin-mediated proteolysis to degrade an inhibitor, a process essential for cell movement and proliferation. Microtubule dynamics influence this degradation, revealing a new regulatory mechanism.

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Area of Science:

Cell Biology
Molecular Biology

Background:

Cellular contractility is crucial for cell movement and proliferation, regulated by microtubules, RhoA, and actomyosin.
Microtubules inhibit contractility, and their depolymerization activates RhoA, but the precise regulation remains unclear.

Purpose of the Study:

To investigate the role of microtubule dynamics in regulating cellular contractility.
To identify the molecular mechanisms underlying microtubule-mediated inhibition of contractility.

Main Methods:

Observation of cellular contractility in adherent and non-adhering cells.
Inhibition of proteolysis, ubiquitination, and neddylation pathways.
Measurement of Myosin II Light Chain (MLC) Ser19 phosphorylation.

Main Results:

Microtubules inhibit contractility in both adherent and non-adhering cells.
Contractility requires ubiquitin-mediated proteolysis by a Cullin-RING ubiquitin ligase.
Inhibiting proteolysis, ubiquitination, or neddylation halted contractility and reduced MLC Ser19 phosphorylation.

Conclusions:

Cells possess a contractility inhibitor degraded via ubiquitin-mediated proteolysis.
This degradation, dependent on a Cullin-RING ubiquitin ligase, is necessary for cellular contractions.
Microtubule depolymerization may trigger this degradation pathway.