Dropping anchor: Stringent quality control prevents GPI anchoring of severely misfolded proteins in plants

Research output: Contribution to journalComment/debatepeer-review

Abstract

To survive, organisms must carefully control the levels and activities of thousands of proteins that make up their cellular proteome. Protein homeostasis, often termed proteostasis, is maintained by the complex interplay between protein synthesis, folding, and degradation. In eukaryotes, the endoplasmic reticulum (ER) plays a central role in proteostasis as the site where proteins undergo folding and maturation before being transported to their final cellular destination. Incorrectly folded proteins are usually recognized by ER quality control (ERQC) mechanisms and rapidly subjected to ER-associated degradation (ERAD; Berner et al., 2018). However, if misfolded proteins are not efficiently cleared, this can lead to their accumulation and clumping together to form protein aggregates. In animals, protein aggregation can result in formation of stable fibrillar structures, known as amyloids, that are the underlying cause of many human neurodegenerative conditions, including amyotrophic lateral sclerosis (ALS), Alzheimer’s, and Parkinson’s disease (Davis et al., 2018).
Original languageEnglish
Pages (from-to)1757-1759
Number of pages4
JournalPlant physiology
Volume186
Issue number4
DOIs
Publication statusPublished - 29 Jul 2021

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