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Related Concept Videos

Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

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Related Experiment Video

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Using CRISPR/Cas9 Gene Editing to Investigate the Oncogenic Activity of Mutant Calreticulin in Cytokine Dependent Hematopoietic Cells
10:21

Using CRISPR/Cas9 Gene Editing to Investigate the Oncogenic Activity of Mutant Calreticulin in Cytokine Dependent Hematopoietic Cells

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Mutational analysis of calnexin.

Jody Groenendyk1, Monika Dabrowska, Marek Michalak

  • 1Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada.

Biochimica Et Biophysica Acta
|April 14, 2010
PubMed
Summary

Mutations in calnexin, an endoplasmic reticulum chaperone, impaired its ability to prevent protein aggregation. Specific mutations also altered binding to the folding enzyme ERp57, impacting calnexin

Area of Science:

  • Molecular Biology
  • Protein Folding
  • Endoplasmic Reticulum Biology

Background:

  • Calnexin is a crucial lectin-like chaperone protein in the endoplasmic reticulum.
  • It plays a vital role in the proper folding and quality control of glycoproteins.

Purpose of the Study:

  • To investigate the functional significance of specific residues in calnexin.
  • To understand the impact of mutations on calnexin's interaction with substrates and folding enzymes.

Main Methods:

  • Site-specific mutagenesis was employed to alter key residues in calnexin.
  • The functional consequences of these mutations were assessed using glycosylated substrates and ERp57 binding assays.

Main Results:

  • Calnexin mutants with alterations at E351 and W428 lost their ability to inhibit IgY aggregation.

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  • Mutation W428 significantly enhanced the binding of ERp57 to calnexin, while E351 showed a slight enhancement.
  • These findings suggest that residues in the carbohydrate-binding region critically influence calnexin's P-domain function and ERp57 association.

    • Conclusions:

    • The study highlights the importance of specific residues in calnexin's structure and function.
    • Alterations in the carbohydrate-binding region can profoundly affect calnexin's chaperone activity and interaction with ERp57.
    • These insights contribute to understanding protein quality control mechanisms within the endoplasmic reticulum.