EDEM contributes to maintenance of protein folding efficiency and secretory capacity

KK Eriksson, R Vago, V Calanca, C Galli… - Journal of Biological …, 2004 - ASBMB
A stringent quality control process selects misfolded polypeptides generated in the
endoplasmic reticulum (ER) for ER-associated degradation (ERAD). Here we assessed the …

The role of lectin-carbohydrate interactions in the regulation of ER-associated protein degradation

M Słomińska-Wojewódzka, K Sandvig - Molecules, 2015 - mdpi.com
Proteins entering the secretory pathway are translocated across the endoplasmic reticulum
(ER) membrane in an unfolded form. In the ER they are restricted to a quality control system …

Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation

ED Spear, DTW Ng - The Journal of cell biology, 2005 - rupress.org
The endoplasmic reticulum (ER) maintains an environment essential for secretory protein
folding. Consequently, the premature transport of polypeptides would be harmful to the cell …

A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation

S Olivari, C Galli, H Alanen, L Ruddock… - Journal of Biological …, 2005 - ASBMB
Proteins expressed in the endoplasmic reticulum (ER) are subjected to a tight quality control.
Persistent association with ER-resident molecular chaperones prevents exit of misfolded or …

Glycan regulation of ER-associated degradation through compartmentalization

R Benyair, N Ogen-Shtern, GZ Lederkremer - Seminars in cell & …, 2015 - Elsevier
The internal environment of the eukaryotic cell is divided by membranes into various
organelles, containing diverse functional subcompartments, which allow complex cellular …

EDEM1 recognition and delivery of misfolded proteins to the SEL1L-containing ERAD complex

JH Cormier, T Tamura, JC Sunryd, DN Hebert - Molecular cell, 2009 - cell.com
Terminally misfolded or unassembled secretory proteins are retained in the endoplasmic
reticulum (ER) and subsequently cleared by the ER-associated degradation (ERAD) …

EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming

K Hirao, Y Natsuka, T Tamura, I Wada, D Morito… - Journal of Biological …, 2006 - ASBMB
Quality control in the endoplasmic reticulum ensures that only properly folded proteins are
retained in the cell through mechanisms that recognize and discard misfolded or …

[HTML][HTML] A novel ER α‐mannosidase‐like protein accelerates ER‐associated degradation

N Hosokawa, I Wada, K Hasegawa, T Yorihuzi… - EMBO …, 2001 - embopress.org
The quality control mechanism in the endoplasmic reticulum (ER) discriminates correctly
folded proteins from misfolded polypeptides and determines their fate. Terminally misfolded …

Lectin-like ERAD players in ER and cytosol

Y Yoshida, K Tanaka - Biochimica et Biophysica Acta (BBA)-General …, 2010 - Elsevier
Protein quality control in the endoplasmic reticulum (ER) is an elaborate process conserved
from yeast to mammals, ensuring that only newly synthesized proteins with correct …

The mammalian UPR boosts glycoprotein ERAD by suppressing the proteolytic downregulation of ER mannosidase I

DJ Termine, KW Moremen… - Journal of cell …, 2009 - journals.biologists.com
The secretory pathway provides a physical route through which only correctly folded gene
products are delivered to the eukaryotic cell surface. The efficiency of endoplasmic reticulum …