N-linked oligosaccharides as outfitters for glycoprotein folding, form and function

Mitra, Nivedita; Sinha, Sharmistha; Ramya, Thirumalai N.C.; Surolia, Avadhesha

doi:10.1016/j.tibs.2006.01.003

Cited by 302Glycosylation and Glycoproteins ResearchViral Infectious Diseases and Gene Expression in InsectsCarbohydrate Chemistry and Synthesis

N-linked oligosaccharides as outfitters for glycoprotein folding, form and function

Mitra, Nivedita, Sinha, Sharmistha, Ramya, Thirumalai N.C., Surolia, Avadhesha·2006·Trends in Biochemical Sciences

DOI 10.1016/j.tibs.2006.01.003

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Abstract

Glycosylation, particularly N-linked glycosylation, profoundly affects protein folding, oligomerization and stability. The increased efficiency of folding of glycosylated proteins could be due to the chaperone-like activity of glycans, which is observed even when the glycan is not attached to the protein. Covalently linked glycans could also facilitate oligomerization by mediating inter-subunit interactions in the protein or stabilizing the oligomer in other ways. Glycosylation also affects the rate of fibril formation in prion proteins: N-glycans reduce the rate of fibril formation, and O-glycans affect the rate either way depending on factors such as position and orientation. It has yet to be determined whether there is any correlation among the sites of glycosylation and the ensuing effect in multiply glycosylated proteins. It is also not apparent whether there is a common pattern in the conservation of glycans in a related family of glycoproteins, but it is evident that glycosylation is a multifaceted post-translational modification. Indeed, glycosylation serves to "outfit" proteins for fold-function balance.

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Authors: Mitra, N., Sinha, S., Ramya, T. N. C., & Surolia, A.
Affiliations: Indian Institute of Science Bangalore (IN)
Corresponding author: Surolia, Avadhesha
ORCID: Mitra, Nivedita
Sinha, Sharmistha
Ramya, Thirumalai N.C.
Surolia, Avadhesha
Venue: Trends in Biochemical Sciences
Publisher: Elsevier BV
Published: 2006-03
Volume: 31
Issue: 3
Pages: 156-163
ISSN: 0968-0004 (ISSN-L)
DOI: 10.1016/j.tibs.2006.01.003
OpenAlex: W1979729411
Cited by: 302
References: 79
Citations by year: 2026: 8 · 2025: 8 · 2024: 14 · 2023: 12 · 2022: 15 · 2021: 15 · 2020: 19 · 2019: 12 · 2018: 8 · 2017: 13 · 2016: 17 · 2015: 15 · 2014: 11 · 2013: 19 · 2012: 12
FWCI: 1.83
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Trends in Biochemical Sciences (publishedVersion)
PubMed (publishedVersion)
NOT FOUND REPOSITORY (Indian Institute of Science Bangalore) (acceptedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
Keywords: N-glycosylation, glycoprotein folding, protein oligomerization, protein stability, O-glycosylation, glycosylation sites, post-translational modification
MeSH terms: Animals, Glycoproteins, Humans, Models, Biological, Oligosaccharides, Protein Binding, Protein Denaturation, Protein Folding

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N-linked oligosaccharides as outfitters for glycoprotein folding, form and function

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