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Mammalian sugar‐binding receptors: known functions and unexplored roles
Author(s) -
Taylor Maureen E.,
Drickamer Kurt
Publication year - 2019
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.14759
Subject(s) - glycan , receptor , glycoprotein , biology , glycolipid , microbiology and biotechnology , innate immune system , glycobiology , biochemistry , galectin , computational biology
Mammalian glycan‐binding receptors, sometimes known as lectins, interact with glycans, the oligosaccharide portions of endogenous mammalian glycoproteins and glycolipids as well as sugars on the surfaces of microbes. These receptors guide glycoproteins out of and back into cells, facilitate communication between cells through both adhesion and signaling, and allow the innate immune system to respond quickly to viral, fungal, bacterial, and parasitic pathogens. For many of the roughly 100 glycan‐binding receptors that are known in humans, there are good descriptions of what types of glycans they bind and how selectivity for these ligands is achieved at the molecular level. In some cases, there is also comprehensive evidence for the roles that the receptors play at the cellular and organismal levels. In addition to highlighting these well‐understood paradigms for glycan‐binding receptors, this review will suggest where gaps remain in our understanding of the physiological functions that they can serve.