TY - JOUR
T1 - Glycoprotein folding, quality control and ER-associated degradation
AU - Lederkremer, Gerardo Z.
N1 - Funding Information:
I thank Edward Avezov and Ron Benyair for helpful comments. I apologize to authors whose work I was unable to cite owing to space limitations. Research related to this work is supported by grants from the Israel Science Foundation (1229/07), German-Israeli Project Cooperation (DIP), Israel Cancer Association and Kodesz Institute.
PY - 2009/10
Y1 - 2009/10
N2 - Nascent N-linked glycoproteins possess a large oligosaccharide precursor, Glc3Man9GlcNAc2, which is later sequentially trimmed. Recent studies help understand the code displayed by each structure produced by this trimming and its decoding by lectins. The calnexin folding cycle targets only monoglucosylated oligosaccharides. N-glycans of misfolded glycoproteins are then more extensively trimmed than once thought, being targeted for degradation by removal of three or four mannose residues. A high local concentration of endoplasmic reticulum (ER) mannosidase I in an ER-derived quality control compartment is mainly responsible for this trimming, with the possible participation of other mannosidases. The shortened chains, Man5-6GlcNAc2, are recognized by the ubiquitination machinery-associated lectin OS9 but not by lectins that associate with properly folded glycoproteins en route to the Golgi that bind best to Man8-9GlcNAc2.
AB - Nascent N-linked glycoproteins possess a large oligosaccharide precursor, Glc3Man9GlcNAc2, which is later sequentially trimmed. Recent studies help understand the code displayed by each structure produced by this trimming and its decoding by lectins. The calnexin folding cycle targets only monoglucosylated oligosaccharides. N-glycans of misfolded glycoproteins are then more extensively trimmed than once thought, being targeted for degradation by removal of three or four mannose residues. A high local concentration of endoplasmic reticulum (ER) mannosidase I in an ER-derived quality control compartment is mainly responsible for this trimming, with the possible participation of other mannosidases. The shortened chains, Man5-6GlcNAc2, are recognized by the ubiquitination machinery-associated lectin OS9 but not by lectins that associate with properly folded glycoproteins en route to the Golgi that bind best to Man8-9GlcNAc2.
UR - http://www.scopus.com/inward/record.url?scp=70349855203&partnerID=8YFLogxK
U2 - 10.1016/j.sbi.2009.06.004
DO - 10.1016/j.sbi.2009.06.004
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AN - SCOPUS:70349855203
SN - 0959-440X
VL - 19
SP - 515
EP - 523
JO - Current Opinion in Structural Biology
JF - Current Opinion in Structural Biology
IS - 5
ER -