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Related Experiment Video

Updated: Jan 19, 2026

Frustration and Conflict: Avoidance-Avoidance, Double-Approach Avoidance
01:14

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612

How to Avoid a No-Deal ER Exit.

Tiziana Anelli1,2, Paola Panina-Bordignon3,4

  • 1Vita-Salute San Raffaele University, 20132 Milan, Italy. anelli.tiziana@hsr.it.

Cells
|September 11, 2019
PubMed
Summary
This summary is machine-generated.

Proper protein folding and transport from the endoplasmic reticulum (ER) to the Golgi are crucial for cell health. Disruptions in ER quality control or transport can lead to protein accumulation and disease.

Keywords:
COPII vesiclesERGICendoplasmic reticulumprotein foldingtraffic

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Related Experiment Videos

Last Updated: Jan 19, 2026

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Protein secretion involves sequential steps for folding and maturation within the secretory compartment.
  • The endoplasmic reticulum (ER) is key for initial protein folding, aided by chaperones and enzymes.
  • Quality control (QC) mechanisms in the ER permit correctly folded proteins to exit, while misfolded proteins are targeted for degradation.

Purpose of the Study:

  • To review the pathophysiology of protein folding and transport between the ER and Golgi.
  • To elucidate the mechanisms controlling protein folding and maturation in the secretory pathway.
  • To discuss the consequences of impaired ER quality control and transport.

Main Methods:

  • This review synthesizes existing literature on protein folding and trafficking.
  • It examines the roles of chaperones, enzymes, and QC systems in the ER.
  • The review analyzes the process of vesicle-mediated transport from the ER to the Golgi.

Main Results:

  • Misfolded proteins are retained in the ER and degraded via the proteasome.
  • ER exit sites facilitate the formation of coated vesicles for protein transport to the Golgi.
  • Dysfunctional ER QC or transport leads to protein accumulation, potentially causing cellular damage and disease.

Conclusions:

  • Efficient protein secretion relies on precise folding, maturation, and transport.
  • ER protein accumulation due to QC or transport defects is detrimental to cellular and organismal health.
  • Understanding these processes is vital for comprehending the molecular basis of related diseases.