Cited by 89Glycosylation and Glycoproteins ResearchProtease and Inhibitor MechanismsEnzyme Structure and Function

Recognition of protein-linked glycans as a determinant of peptidase activity

Open access
Noach, Ilit, Ficko-Blean, Elizabeth, Pluvinage, Benjamin, Stuart, Christopher, Jenkins, Meredith L., Brochu, Denis, Buenbrazo, Nakita, Wakarchuk, Warren +3 more·2017·Proceedings of the National Academy of Sciences

Abstract

Significance: Protein glycosylation is one of the most abundant and important posttranslational modifications where the protein-linked glycans can impart specific physiochemical properties to the glycoprotein and/or the glycans themselves can mediate particular biological functions. The degradation of glycosylated proteins in normal or pathogenic processes, therefore, is an important biological process. This study reveals the molecular basis of how peptidases can use the O-glycans present on glycoproteins as a critical determinant of peptidase activity and, in doing so, provides unique insight into how peptidases may directly use posttranslational modifications present on their substrates to influence recognition and peptide bond cleavage.

Integrity signals

Registry

Crossref · 10.1073/pnas.1615141114

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50 of 50 references verified0 citation errors · 0 not checkable

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  • Different mucin-degrading proteases have been described in Bacteroides, a common commensal of the human intestine.

    “Different mucin-degrading proteases have been also described in Bacteroides, a common commensal of the human intestine.”
  • Mucin-degrading proteases in Bacteroides include proteases in B. thetaiotaomicron (BT4244) or Bacteroides caccae.

    “These include proteases in B. thetaiotaomicron (BT4244) or Bacteroides caccae.126,127”
  • The M60-like protease family cleaves the mucin glycoprotein backbone in a manner dependent on the presence of specific glycan sidechain structures.

    “the M60-like protease family cleaves the mucin glycoprotein backbone in a manner that is dependent on the presence of specific glycan sidechain structures.125,126”

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Authors
Noach, I., Ficko-Blean, E., Pluvinage, B., Stuart, C., Jenkins, M. L., Brochu, D., Buenbrazo, N., Wakarchuk, W., Burke, J. E., Gilbert, M., & Boraston, A. B.
Affiliations
  • University of Victoria (CA)
  • Department of Biochemistry and Microbiology, University of Victoria, Victoria, BC V8W 3P6, Canada;
  • National Research Council Canada (CA)
  • Toronto Metropolitan University (CA)
Venue
Proceedings of the National Academy of Sciences
Published
2017-01-17
Volume
114
Issue
5
Pages
E679-E688
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2579867384
Cited by
89
References
50
Citations by year
2026: 10 · 2025: 9 · 2024: 10 · 2023: 10 · 2022: 18 · 2021: 6 · 2020: 14 · 2019: 9 · 2018: 3
FWCI
2.90
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • HAL (submittedVersion)
  • NPARC (submittedVersion)
Funders
  • Gouvernement du Canada | Canadian Institutes of Health Research (MOP 130305)
  • Gouvernement du Canada | Natural Sciences and Engineering Research Council of Canada (NSERC‐2014‐05218)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
O-glycosylation, metalloproteinases, post-translational modification, glycoprotein degradation, peptide bond cleavage
MeSH terms
Escherichia coli, Glycopeptides, Glycosylation, Mucins, Peptide Hydrolases, Polysaccharides, Protein Conformation, Protein Processing, Post-Translational, Fetuins

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