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Related Experiment Videos

Lectins as chaperones in glycoprotein folding

E S Trombetta1, A Helenius

  • 1Department of Cell Biology, Yale Medical School, New Haven, CT 06520-8002, USA. sergio.trombetta@yale.edu

Current Opinion in Structural Biology
|November 18, 1998
PubMed
Summary

Newly synthesized glycoproteins interact with the calnexin/calreticulin chaperone system in the endoplasmic reticulum. This interaction, crucial for glycoprotein folding and quality control, is mediated by transiently monoglucosylated oligosaccharides.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Biology

Background:

  • N-glycosylation is a critical post-translational modification for newly synthesized proteins.
  • The endoplasmic reticulum (ER) houses a specialized chaperone system for glycoproteins.
  • Lectin chaperones, such as calnexin and calreticulin, play a key role in ER protein quality control.

Purpose of the Study:

  • To elucidate the mechanism by which glycoproteins interact with the ER lectin chaperone system.
  • To understand the role of oligosaccharide modifications in glycoprotein folding and maturation.
  • To highlight the specific chaperone functions of calnexin and calreticulin in the ER.

Main Methods:

  • Investigating the transient deglucosylation and reglucosylation of oligosaccharides on substrate glycoproteins.

Related Experiment Videos

  • Analyzing the binding interactions between monoglucosylated glycoproteins and lectin chaperones (calnexin, calreticulin).
  • Studying the impact of this chaperone system on glycoprotein folding and oligomerization in mammalian cells.

    • Main Results:

    • Monoglucosylated oligosaccharides transiently produced during glycoprotein maturation mediate binding to calnexin and calreticulin.
    • This transient binding facilitates the interaction of glycoproteins with the lectin-based chaperone system.
    • Calnexin, calreticulin, and associated factors are essential for correct glycoprotein folding and oligomerization within the ER.

    Conclusions:

    • The monoglucosylation-dependent interaction with calnexin and calreticulin is a key mechanism for glycoprotein quality control in the ER.
    • This lectin-based system provides specific chaperone functions essential for proper glycoprotein maturation.
    • Understanding this process is vital for comprehending protein homeostasis and function within the endoplasmic reticulum.