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Michael Scott Boyce

Associate Professor of Biochemistry
Biochemistry
Box 3711, Durham, NC 27710
208A Nanaline H Duke, Durham, NC 27710

Overview


The Boyce Lab studies mammalian cell signaling through protein glycosylation. For the latest news, project information and publications from our group, please visit our web site at http://www.boycelab.org or follow us on Twitter at https://twitter.com/BoyceLab.

Current Appointments & Affiliations


Associate Professor of Biochemistry · 2019 - Present Biochemistry, Basic Science Departments
Associate Professor of Cell Biology · 2022 - Present Cell Biology, Basic Science Departments
Member of the Duke Cancer Institute · 2014 - Present Duke Cancer Institute, Institutes and Centers

In the News


Published July 8, 2019
White House Honors Four Faculty for Early Career Research Accomplishments
Published July 2, 2019
White House announces PECASE winners
Published October 16, 2013
1,100: Night Lights

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Recent Publications


Dynamic O-GlcNAcylation of Sec23-interacting protein regulates COPII function.

Journal Article bioRxiv · December 20, 2025 About one-third of the eukaryotic proteome transits the secretory pathway to reach its correct cellular or extracellular destination. At the earliest stage, transport from the endoplasmic reticulum (ER) to the ER-Golgi intermediate compartment (ERGIC) or G ... Full text Link to item Cite

Evidence for functional regulation of the KLHL3/WNK pathway by O-GlcNAcylation.

Journal Article Glycobiology · August 11, 2025 The 42-member Kelch-like (KLHL) protein family are adaptors for ubiquitin E3 ligase complexes, governing the stability of a wide range of substrates. KLHL proteins are critical for maintaining proteostasis in a variety of tissues and are mutated in human d ... Full text Link to item Cite

Dynamic regulation of Sec24C by phosphorylation and O-GlcNAcylation during cell cycle progression.

Journal Article J Biol Chem · August 2025 During mitosis, eukaryotic cells cease anterograde trafficking from the endoplasmic reticulum (ER) toward the Golgi. This cessation corresponds with the dispersal of the COPII transport protein, Sec24C, from juxtanuclear ER exit sites (ERES) into a diffuse ... Full text Link to item Cite
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Recent Grants


Cell signaling through O-linked glycosylation

ResearchPrincipal Investigator · Awarded by National Institutes of Health · 2026 - 2031

Pharmacological Sciences Training Program

Inst. Training Prgm or CMEPreceptor · Awarded by National Institutes of Health · 2025 - 2030

The Duke Preparing Research scholars In bioMEdical sciences (PRIME): Cancer Research Program

ResearchPreceptor · Awarded by National Cancer Institute · 2023 - 2028

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Education


Harvard Medical School · 2005 Ph.D.