Abstract 1709 Understanding How Proteins are Extracted from the ER Lectin Chaperone Cycle for Degradation
One third of the human proteome is targeted to the secretory pathway and translocated into the endoplasmic reticulum (ER). This organelle provides the environment necessary for the proper folding of proteins prior to trafficking. Many clients of the secretory pathway are appended with carbohydrates, known as N-linked glycans that act as quality control tags. These glycans are added co- or post-translationally and rapidly modified to allow the protein to bind the lectin chaperones, calnexin and calreticulin.
Authors
- Kaifu Ke (ORCID: https://orcid.org/0000-0002-5717-8681)
- Daniel N. Hebert (ORCID: https://orcid.org/0000-0003-1537-4446)
- Kevin P. Guay (ORCID: https://orcid.org/0000-0002-3468-942X)
- Elena L. Pobezinskaya (ORCID: https://orcid.org/0000-0001-6408-8732)
Institutions
- University of Massachusetts Amherst (US)
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.108813
- Primary Topic
- Endoplasmic Reticulum Stress and Disease
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Institutes of Health
- University of Massachusetts Amherst