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Related Concept Videos

The Proteasome01:13

The Proteasome

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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...
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Regulated Protein Degradation02:58

Regulated Protein Degradation

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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...
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Covalently Linked Protein Regulators02:04

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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Receptor Downregulation in MVBs01:15

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Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
The EGFR can initiate signaling pathways that  lead to cell proliferation, migration, and differentiation. Overexpression of EGFR  stimulates cells to proliferate. Excessive  EGFR...
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Anaphase Promoting Complex00:50

Anaphase Promoting Complex

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The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...
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The Proteasome Structure01:17

The Proteasome Structure

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The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
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Related Experiment Video

Updated: May 23, 2025

Method for Measuring the Activity of Deubiquitinating Enzymes in Cell Lines and Tissue Samples
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Deubiquitinases and Cancer.

Preethi Murali1, B Kavitha1, Malathi Narasimhan2

  • 1Department of Oral and Maxillofacial Pathology and Oral Microbiology, Meenakshi Ammal Dental College and Hospital, MAHER, Chennai, Tamil Nadu, India.

Journal of Pharmacy & Bioallied Sciences
|March 10, 2025
PubMed
Summary
This summary is machine-generated.

Deubiquitinases (DUBs) remove ubiquitin from proteins, regulating crucial cellular functions. Aberrant DUBs are implicated in cancer development and progression, offering potential therapeutic targets.

Keywords:
ApoptosisDUB’scancer-related pathway

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Biology

Background:

  • Deubiquitinases (DUBs) are enzymes that remove ubiquitin (UBQ) from ubiquitylated substrates.
  • DUBs regulate diverse cellular processes including proteolysis, gene expression, cell cycle, DNA damage repair, and immunity.
  • Dysregulation of DUBs is linked to various human diseases, particularly cancer.

Purpose of the Study:

  • To review the fundamental role of DUBs in cellular functions.
  • To explore the involvement of DUBs in carcinogenesis and cancer development.
  • To highlight DUBs' significance in T-cell development, apoptosis, and oral cancers.

Main Methods:

  • Literature review of DUBs' functions in cellular processes.
  • Analysis of DUBs' involvement in cancer biology, immunity, and disease.
  • Focus on recent advances in DUBs' role in tumorigenesis and therapeutic potential.

Main Results:

  • DUBs are critical regulators of protein stability and activity, impacting numerous cellular pathways.
  • Aberrant DUB expression contributes to cancer hallmarks like proliferation, metastasis, and immune evasion.
  • DUBs play a key role in T-cell function and apoptosis, with implications for oral cancer.

Conclusions:

  • DUBs are essential for normal cellular functions and immune responses.
  • The dysregulation of DUBs is a significant driver of cancer development.
  • Targeting DUBs presents a promising therapeutic strategy for various cancers, including oral cancers.