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Yos9, a control protein for misfolded glycosylated and non‐glycosylated proteins in ERAD
Author(s) -
Martinez Benitez Elena,
Stolz Alexandra,
Wolf Dieter H.
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.08.021
Subject(s) - endoplasmic reticulum associated protein degradation , endoplasmic reticulum , glycosylation , glycan , protein folding , microbiology and biotechnology , chemistry , cytoplasm , secretory pathway , protein degradation , biochemistry , secretory protein , glycoprotein , protein sorting signals , signal peptide , biology , unfolded protein response , secretion , golgi apparatus , peptide sequence , gene
The endoplasmic reticulum (ER) is responsible for folding and delivery of secretory proteins to their site of action. One major modification proteins undergo in this organelle is N‐glycosylation. Proteins that cannot fold properly will be directed to a process known as endoplasmic reticulum associated degradation (ERAD). Processing of N‐glycans generates a signal for ERAD. The lectin Yos9 recognizes the N‐glycan signal of misfolded proteins and acts as a gatekeeper for the delivery of these substrates to the cytoplasm for degradation. Presence of Yos9 accelerates degradation of the glycosylated model ERAD substrate CPY ∗ . Here we show that Yos9 has also a control function in degradation of the unglycosylated ERAD substrate CPY ∗ 0000. It decelerates its degradation rate.