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Related Concept Videos

Caspases01:24

Caspases

Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside cells.
The Proteasome02:18

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 Proteasome01:13

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 Proteasome02:18

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 Structure01:17

The Proteasome Structure

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...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...

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Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader
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Published on: May 24, 2024

The proprotein convertases, 20 years later.

Nabil G Seidah1

  • 1Biochemical Neuroendocrinology Laboratory, Clinical Research Institute of Montreal, Montreal, QC, Canada H2W 1R7. nabil.seidah@ircm.qc.ca

Methods in Molecular Biology (Clifton, N.J.)
|August 2, 2011
PubMed
Summary
This summary is machine-generated.

Proprotein convertases (PCs) are crucial serine proteases involved in cellular biology and communication. Further research is needed to fully understand their complex roles in health and disease, including potential therapeutic applications.

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Last Updated: May 30, 2026

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Enzymology

Background:

  • Proprotein convertases (PCs) are a family of nine secretory mammalian serine proteinases.
  • These enzymes are related to bacterial subtilisin-like enzymes and play diverse roles in cellular processes.
  • While initially challenging to identify, all nine PC members were characterized within 14 years.

Observation:

  • Seven PCs cleave after basic residues, while two cleave at non-basic residues.
  • PCSK9, the final member, uniquely cleaves itself for activation.
  • The targets and substrates of PCs are highly varied, impacting cellular biology and communication.

Findings:

  • Significant progress has been made in characterizing the PC family and their substrates.
  • Current understanding of PC physiological functions in health and disease is still evolving.
  • Key questions remain regarding in vivo mechanisms, regulatory partners, and substrate identification.

Implications:

  • Understanding PCs could lead to novel therapeutic strategies for various pathologies.
  • Investigating human genetic variations (SNPs/mutations) in PCs may elucidate their functions and disease correlations.
  • Future research promises new insights into the biology of these ancient proteases and their cellular trafficking pathways.