Boyce Lab
Principal Investigator: Michael S Boyce
Institution: Duke University (Durham, NC)
Primary Subfield: Molecular & Cell Bio
Recruitment Status: Inquire for rotation/fellowship opportunities
Research Focus
Project Summary/Abstract Glycosylation – the enzymatic attachment of carbohydrates onto biomolecules – is the most abundant post-translational modification (PTM) of proteins in nature. In mammals, glycosylation influences all aspects of cell biology, including protein quality control and secretion, intracellular signaling, membrane composition and fluidity, cell adhesion and migration, cell-cell communication, and organogenesis. Aberrant glycosylation also underlies a wide range of human diseases, such as developmental defects, obesity and metabolic syndrome, cancer, neurodegeneration, and atherosclerosis. Despite its significance, protein glycosylation remains an under-studied aspect of cell biology, due partly to the unique challenges in characterizing it. Indeed, protein glycosylation is heterogeneous, chemically complex, and created ab initio, without a template molecule, unlike DNA, RNA, or protein biosynthesis. New, interdisciplinary approaches are needed to understand protein glycosylation in physiology and disease. My research program focuses on protein O-glycosylation (i.e., glycans modifying serine and threonine side-chains). In particular, we have a longstanding interest…
Active NIH Awards
- 1R35GM161290-01: Cell signaling through O-linked glycosylation (2026)
- 1R01NS148075-01: Metabolic regulation of KLHL proteins and targets through O-glycosylation (2026)
- 5R01GM118847-09: Cell signaling through O-GlcNAc reader proteins (2025)
- 5R01GM117473-08: Control of COPII vesicle trafficking by intracellular protein glycosylation (2025)
- 5R01GM117473-07: Control of COPII vesicle trafficking by intracellular protein glycosylation (2024)
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