Skaggs Graduate School of Chemical and Biological Sciences, Scripps Research, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA; Department of Molecular Medicine, Scripps Research, 120 Scripps Way, Jupiter, FL 33458, USA; Department of Molecular Medicine, Scripps Research, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA.
Department of Molecular Medicine, Scripps Research, 120 Scripps Way, Jupiter, FL 33458, USA; Department of Molecular Medicine, Scripps Research, 10550 N Torrey Pines Road, La Jolla, CA 92037, USA.
Trends Biochem Sci. 2022 Jun;47(6):492-505. doi: 10.1016/j.tibs.2022.02.007. Epub 2022 Mar 17.
Post-translational modifications (PTMs) immensely expand the diversity of the proteome. Glycosylation, among the most ubiquitous PTMs, is a dynamic and multifarious modification of proteins and lipids that generates an omnipresent foliage on the cell surface. The resulting protein glycoconjugates can serve important functions in biology. However, their vast complexity complicates the study of their structures, interactions, and functions. There is now a growing appreciation of the need to study glycans and proteins together as complete entities, as the sum of these two components can exhibit unique functions. In this review, we discuss the growing forestry toolbox to characterize the structure, interactions, and biological functions of protein glycoconjugates, as well as the potential payouts of understanding and controlling these enigmatic biomolecules.
