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Related Concept Videos

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 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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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...

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Related Experiment Video

Updated: Jun 21, 2026

Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry

Published on: November 12, 2012

PCI complexes: Beyond the proteasome, CSN, and eIF3 Troika.

Elah Pick1, Kay Hofmann, Michael H Glickman

  • 1Department of Biology, Haifa University at Oranim, Tivon, Israel. elahpic@research.haifa.ac.il

Molecular Cell
|August 18, 2009
PubMed
Summary

The PCI domain is a key scaffold in protein complexes like the proteasome, CSN, and eIF3, influencing protein lifespan. It also participates in nucleic acid regulation, highlighting the extended PCI family

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Identification of Protein Complexes in Escherichia coli using Sequential Peptide Affinity Purification in Combination with Tandem Mass Spectrometry
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Published on: November 12, 2012

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09:57

Examining Proteasome Assembly with Recombinant Archaeal Proteasomes and Nondenaturing PAGE: The Case for a Combined Approach

Published on: December 17, 2016

Area of Science:

  • Molecular Biology
  • Protein Biochemistry
  • Genetics

Background:

  • The proteasome, CSN (Cullin-Nedd8), and eIF3 (eukaryotic initiation factor 3) are crucial protein complexes involved in cellular regulation.
  • PCI domains are conserved structural modules found in these and other protein complexes.
  • Understanding the role of PCI domains is essential for comprehending protein homeostasis and gene expression.

Purpose of the Study:

  • To elucidate the structural and functional significance of the bipartite PCI domain.
  • To investigate the role of PCI domains in diverse protein complexes, including those involved in protein degradation and nucleic acid regulation.
  • To identify shared subunits that facilitate the assembly of the extended PCI protein family.

Main Methods:

  • Bioinformatic analysis of protein domain families.
  • Structural biology techniques to determine complex architecture.
  • Biochemical assays to assess complex assembly and function.

Main Results:

  • The bipartite PCI domain acts as a central scaffold for proteasome lid, CSN, and eIF3 complexes.
  • PCI domains are implicated in newly identified complexes involved in nucleic acid regulation.
  • The Sem1/DSS1 subunit is a common factor that facilitates the assembly of the extended PCI family.

Conclusions:

  • The PCI domain family is functionally diverse, spanning roles in protein lifespan regulation and nucleic acid processing.
  • Shared subunits, such as Sem1/DSS1, are critical for the assembly and function of diverse PCI-containing complexes.
  • The extended PCI family represents a conserved mechanism for organizing cellular regulatory complexes.