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Related Concept Videos

Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Introduction to Membrane Traffic01:44

Introduction to Membrane Traffic

The ER, Golgi apparatus, endosomes, and lysosomes work in tandem to modify, sort, and package proteins and lipids. An integrated membrane trafficking network facilitates the back and forth shuttling of molecules within different organelles in the same cell or across the cell membrane.
The transport of soluble and membrane proteins is mediated by transport vesicles that collect cargo from one cellular compartment and deliver it to another by fusing with the target organelle membrane. The Rab...
Regulated Protein Degradation02:58

Regulated Protein Degradation

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...
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...
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

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Related Experiment Video

Updated: Jun 28, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Ubiquitin in trafficking: the network at work.

Filippo Acconcia1, Sara Sigismund, Simona Polo

  • 1IFOM Foundation, The FIRC Institute for Molecular Oncology, Via Adamello 16, 20139 Milan, Italy.

Experimental Cell Research
|November 15, 2008
PubMed
Summary

Ubiquitination signals protein sorting for intracellular trafficking. This process is crucial for receptor tyrosine kinase (RTK) endocytosis, directing proteins to lysosomes or recycling them to the cell surface.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Membrane protein targeting relies on specific intracellular trafficking mechanisms.
  • Endocytosis of transmembrane receptors, like receptor tyrosine kinases (RTKs), involves internalization and delivery to endosomes.
  • Sorting of these receptors is regulated by protein motifs and post-translational modifications.

Purpose of the Study:

  • To provide an overview of ubiquitin's role in intracellular trafficking.
  • To highlight the mechanisms of ubiquitin-regulated RTK endocytosis.

Main Methods:

  • Literature review on ubiquitination and protein trafficking.
  • Analysis of studies detailing RTK endocytosis pathways.
  • Examples of ubiquitin's regulatory functions in receptor sorting.

Main Results:

  • Ubiquitination serves as a key signal for the internalization and sorting of plasma membrane proteins.
  • Ubiquitin's role in intracellular trafficking is multifaceted.
  • Specific examples illustrate ubiquitin's regulation of RTK endocytosis.

Conclusions:

  • Ubiquitination is a critical post-translational modification controlling protein sorting during endocytosis.
  • Understanding ubiquitin's role is essential for deciphering RTK trafficking pathways.
  • This review consolidates current knowledge on ubiquitin-mediated regulation of RTK endocytosis.