Demystifying Heparan Sulfate–Protein Interactions

By Ding Xu, J. Esko. Annual Review of Biochemistry, 2014

685 citations recorded by the source corpus.

Numerous proteins, including cytokines and chemokines, enzymes and enzyme inhibitors, extracellular matrix proteins, and membrane receptors, bind heparin. Although they are traditionally classified as heparin-binding proteins, under normal physiological conditions these proteins actually interact with the heparan sulfate chains of one or more membrane or extracellular proteoglycans. Thus, they are more appropriately classified as heparan sulfate–binding proteins (HSBPs). This review provides an overview of the various modes of interaction between heparan sulfate and HSBPs, emphasizing biochemical and structural insights that improve our understanding of the many biological functions of heparan sulfate.

Subfields: Cancer Research, Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/f94a99fd33b7df85cc9ac49cf0db902b2c0b11b6

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In Cell Biology

1. J. Esko

In Molecular Biology

1. A. Ward
2. J. Esko
3. Cameron Martino

Citations in the corpus

• SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2 (2020, background): “The variable length of the modified domains and their pattern of sulfation create unique motifs to which HS-binding proteins interact (Xu and Esko, 2014).”
• SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2 (2020, positive): “The variable length of the modified domains and their pattern of sulfation create unique motifs to which HS-binding proteins (HSBPs) interact (Xu and Esko, 2014).”