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Related Concept Videos

Protein Complex Assembly02:41

Protein Complex Assembly

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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.
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Initiation of Translation02:33

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Initiating translation is complex because it involves multiple molecules. Initiator tRNA, ribosomal subunits, and eukaryotic initiation factors (eIFs) are all required to assemble on the initiation codon of mRNA. This process consists of several steps that are mediated by different eIFs.
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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Coat Assembly and GTPases01:33

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Formation of Intermediate Filaments00:57

Formation of Intermediate Filaments

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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Disassembly of Intermediate Filaments01:35

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Intermediate filaments (IFs) do not undergo spontaneous disassembly. Enzymes, kinases, and phosphatases add and remove phosphates from specific sites to regulate their disassembly. The IF concentration in the cytoplasm also regulates the disassembly. If the concentration crosses a threshold, it activates the protein kinases in the vicinity, allowing the phosphorylation of IFs.
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Related Experiment Video

Updated: Mar 20, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
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Assembly of eIF3 Mediated by Mutually Dependent Subunit Insertion.

M Duane Smith1, Luisa Arake-Tacca2, Adam Nitido1

  • 1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720, USA.

Structure (London, England : 1993)
|May 24, 2016
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Summary

Eukaryotic initiation factor 3 (eIF3) subunits assemble dependently, primarily via a helical bundle. Dysregulated eIF3 subunit expression in cancer may lead to altered complexes, contributing to disease.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Eukaryotic initiation factor 3 (eIF3) is a crucial multi-protein complex regulating translation initiation.
  • While eIF3's overall structure is known, its assembly mechanism and the impact of subunit dysregulation in cancer remain unclear.

Purpose of the Study:

  • To elucidate the assembly mechanism of the human eIF3 complex.
  • To investigate the structural consequences of eIF3 subunit expression dysregulation in cancer.

Main Methods:

  • Analysis of interdependent subunit assembly.
  • Identification of key structural features governing eIF3 formation, including PCI-MPN domains and helical bundles.

Main Results:

  • eIF3 subunits assemble in an interdependent manner.
  • A helical bundle formed by C-terminal helices from PCI-MPN domains is central to eIF3 assembly.
  • A minimal functional eIF3 subcomplex comprises subunits a, b, c, f, g, i, and m.

Conclusions:

  • The assembly of eIF3 is an interdependent process driven by specific structural interactions.
  • Aberrant eIF3 subcomplexes arising from subunit overexpression or underexpression are implicated in cancer development.