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Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the translocon complex.
Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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...
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...

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Updated: May 10, 2026

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells
08:47

Monitoring eIF4F Assembly by Measuring eIF4E-eIF4G Interaction in Live Cells

Published on: May 1, 2020

The E5 proteins.

Daniel DiMaio1, Lisa M Petti

  • 1Department of Genetics, Yale School of Medicine, USA; Department of Therapeutic Radiology, Yale School of Medicine, USA; Department of Molecular Biophysics & Biochemistry, Yale University, USA; Yale Cancer Center, USA.

Virology
|June 5, 2013
PubMed
Summary
This summary is machine-generated.

Human papillomavirus (HPV) E5 oncoproteins are short transmembrane proteins that modulate cellular protein activity. Research highlights their roles in cell transformation and virus replication by targeting key cellular receptors and pathways.

Keywords:
Cervical cancerEGF receptorHPVPDGF receptorPapillomavirusesTransmembrane proteinsVacuolar ATPase

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Area of Science:

  • Molecular biology
  • Virology
  • Cell biology

Background:

  • E5 proteins are short transmembrane proteins encoded by animal and human papillomaviruses.
  • These proteins exhibit transforming activity and are crucial for the productive virus life cycle.
  • E5 proteins are believed to function by modulating the activity of cellular proteins.

Purpose of the Study:

  • To describe the biological activities of well-studied E5 proteins.
  • To discuss specific protein targets and pathways involved in mediating E5 activities.
  • To elucidate aspects of transmembrane protein interactions, signal transduction, and tumorigenesis.

Main Methods:

  • Review of existing literature on E5 protein biological activities.
  • Analysis of evidence implicating specific cellular targets and pathways.
  • Comparison of E5 protein functions across different papillomaviruses.

Main Results:

  • The BPV1 E5 protein primarily targets the PDGF β receptor.
  • The HPV16 E5 protein targets the EGF receptor.
  • Both E5 proteins interact with vacuolar ATPase, affecting MHC class I expression and cell-cell communication.

Conclusions:

  • E5 proteins play significant roles in viral replication and tumorigenesis.
  • Understanding E5 protein interactions provides insights into cellular signaling and transmembrane protein functions.
  • Further research on E5 proteins is essential for understanding virus-host interactions and developing therapeutic strategies.