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Related Concept Videos

Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
Protein sorting can be of two types: signal-based sorting and vesicle-based trafficking. In signal-based sorting, specific amino acid sequences called sorting signals target proteins to the proper location inside the cell either via gated transport or by protein translocation.  In gated transport, folded...
Nuclear Protein Sorting01:34

Nuclear Protein Sorting

Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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...
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...
Protein Transport to the Thylakoids01:22

Protein Transport to the Thylakoids

Thylakoids are membrane-bound sac-like structures within the chloroplast that serve as sites for photosynthesis. Thylakoid lumen contains many electron transport proteins and is enclosed by a thylakoid membrane rich in the light-harvesting complex. Proteins targeted to the thylakoids are transported as precursors and are sorted by the general TOC/TIC import pathway. Once the precursor reaches the stroma, stromal processing peptidases remove their transit signal and expose thylakoid signal...
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...

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Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

Alternative nuclear transport for cellular protein quality control.

April Rose1, Christian Schlieker

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, P.O. Box 208114, Bass 236A, New Haven, CT 06520-8114, USA.

Trends in Cell Biology
|August 4, 2012
PubMed
Summary

Viruses may hijack a cellular pathway for nuclear egress to export large protein aggregates. This pathway could be crucial for clearing cellular waste and understanding nuclear lamina diseases.

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4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

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Last Updated: May 19, 2026

Assays for the Degradation of Misfolded Proteins in Cells
10:56

Assays for the Degradation of Misfolded Proteins in Cells

Published on: August 28, 2016

4D Imaging of Protein Aggregation in Live Cells
08:59

4D Imaging of Protein Aggregation in Live Cells

Published on: April 5, 2013

Area of Science:

  • Cell Biology
  • Virology
  • Molecular Biology

Background:

  • Herpesvirus nuclear egress is a unique viral export pathway.
  • This process involves capsid transport across the nuclear envelope (NE).
  • The nuclear pore complex (NPC) typically limits the size of molecules that can cross the NE.

Purpose of the Study:

  • To investigate if the nuclear egress pathway is an endogenous cellular mechanism.
  • To explore the potential role of this pathway in transporting large cellular cargo.
  • To propose a function for this pathway in clearing nuclear protein aggregates.

Main Methods:

  • Analysis of herpesvirus nuclear egress mechanisms.
  • Hypothesizing the involvement of cellular transport machinery.
  • Modeling the pathway's function in protein aggregate clearance.

Main Results:

  • The nuclear egress pathway may be an ancient cellular mechanism.
  • This pathway could transport cargo larger than the NPC limit.
  • A proposed function is the transport of nuclear protein aggregates for autophagy.

Conclusions:

  • The herpesvirus nuclear egress pathway might be a co-opted cellular pathway.
  • This pathway could serve to eliminate nuclear protein aggregates.
  • Understanding this pathway has implications for nuclear lamina diseases like laminopathies.