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Seeing the forest through the trees: characterizing the glycoproteome
Meg Critcher1, Abdullah A Hassan2, Mia L Huang3
1Skaggs 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.
Trends in Biochemical Sciences
|March 20, 2022
Summary
Post-translational modifications (PTMs) like glycosylation create complex protein glycoconjugates vital for cell functions. New tools help study these structures, interactions, and functions for biological insights.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Post-translational modifications (PTMs) significantly increase proteome diversity.
- Glycosylation is a widespread PTM, creating protein glycoconjugates on cell surfaces with crucial biological roles.
- The complexity of protein glycoconjugates hinders their structural, interaction, and functional studies.
Purpose of the Study:
- To review the expanding toolkit for characterizing protein glycoconjugates.
- To highlight the importance of studying glycans and proteins together.
- To discuss the potential benefits of understanding and controlling these biomolecules.
Main Methods:
- Literature review of current methodologies.
- Discussion of analytical techniques for glycoconjugate characterization.
- Exploration of systems biology approaches.
Main Results:
- A growing array of tools is available for analyzing protein glycoconjugate structure and interactions.
- Integrated approaches are essential for a comprehensive understanding of their functions.
- Characterization of these complex molecules is becoming more feasible.
Conclusions:
- Understanding protein glycoconjugates is crucial for advancing biological and medical sciences.
- Further development of analytical tools will enhance our ability to study these complex biomolecules.
- Controlling protein glycosylation may offer therapeutic potential.
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