Michael Boyce

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.

Positions:

Associate Professor of Biochemistry

Biochemistry
School of Medicine

Member of the Duke Cancer Institute

Duke Cancer Institute
School of Medicine

Education:

Ph.D. 2005

Harvard Medical School

Grants:

Control of COPII vesicle trafficking by intracellular protein glycosylation

Administered By
Biochemistry
Awarded By
National Institutes of Health
Role
Principal Investigator
Start Date
End Date

Protein glycosylation in cancer cell signaling and metabolism

Administered By
Biochemistry
Awarded By
Concern Foundation for Cancer Research
Role
Principal Investigator
Start Date
End Date

Control of COPII vesicle trafficking by intracellular protein glycosylation

Administered By
Biochemistry
Awarded By
National Institutes of Health
Role
Principal Investigator
Start Date
End Date

Control of COPII vesicle trafficking by intracellular protein glycosylation

Administered By
Biochemistry
Awarded By
National Institutes of Health
Role
Principal Investigator
Start Date
End Date

ASCB's MOSAIC Program (AMP)

Administered By
Biochemistry
Awarded By
American Society for Cell Biology
Role
Principal Investigator
Start Date
End Date

Publications:

Evidence for nutrient-dependent regulation of the COPII coat by O-GlcNAcylation.

O-linked β-N-acetylglucosamine (O-GlcNAc) is a dynamic form of intracellular glycosylation common in animals, plants and other organisms. O-GlcNAcylation is essential in mammalian cells and is dysregulated in myriad human diseases, such as cancer, neurodegeneration and metabolic syndrome. Despite this pathophysiological significance, key aspects of O-GlcNAc signaling remain incompletely understood, including its impact on fundamental cell biological processes. Here, we investigate the role of O-GlcNAcylation in the coat protein II complex (COPII), a system universally conserved in eukaryotes that mediates anterograde vesicle trafficking from the endoplasmic reticulum. We identify new O-GlcNAcylation sites on Sec24C, Sec24D and Sec31A, core components of the COPII system, and provide evidence for potential nutrient-sensitive pathway regulation through site-specific glycosylation. Our work suggests a new connection between metabolism and trafficking through the conduit of COPII protein O-GlcNAcylation.
Authors
Bisnett, BJ; Condon, BM; Linhart, NA; Lamb, CH; Huynh, DT; Bai, J; Smith, TJ; Hu, J; Georgiou, GR; Boyce, M
MLA Citation
Bisnett, Brittany J., et al. “Evidence for nutrient-dependent regulation of the COPII coat by O-GlcNAcylation.Glycobiology, vol. 31, no. 9, Sept. 2021, pp. 1102–20. Pubmed, doi:10.1093/glycob/cwab055.
URI
https://scholars.duke.edu/individual/pub1499837
PMID
34142147
Source
pubmed
Published In
Glycobiology
Volume
31
Published Date
Start Page
1102
End Page
1120
DOI
10.1093/glycob/cwab055

Preparing for tenure at a research-intensive university

At research-intensive universities in the United States, eligible faculty must generally excel in research, teaching and service in order to receive tenure. To meet these high standards, junior faculty should begin planning for a strong tenure case from their first day on the job. Here, we provide practical information, commentary and advice on how biomedical faculty at research-intensive institutions can prepare strategically for a successful tenure review.
Authors
Boyce, M; Aguilera, RJ
MLA Citation
Boyce, M., and R. J. Aguilera. “Preparing for tenure at a research-intensive university.” Bmc Proceedings, vol. 15, June 2021. Scopus, doi:10.1186/s12919-021-00221-8.
URI
https://scholars.duke.edu/individual/pub1493456
Source
scopus
Published In
Bmc Proceedings
Volume
15
Published Date
DOI
10.1186/s12919-021-00221-8

Kelch‐like Proteins Have A Sweet Spot: Site‐specific Glycosylation Influences Metabolic Regulation and Protein Homeostasis

Authors
Huynh, DT; Chen, P-H; Hu, J; Smith, TJ; Chi, J-T; Boyce, MS
MLA Citation
Huynh, Duc T., et al. “Kelch‐like Proteins Have A Sweet Spot: Site‐specific Glycosylation Influences Metabolic Regulation and Protein Homeostasis.” The Faseb Journal, vol. 34, no. S1, Wiley, 2020, pp. 1–1. Crossref, doi:10.1096/fasebj.2020.34.s1.00674.
URI
https://scholars.duke.edu/individual/pub1467796
Source
crossref
Published In
Faseb Journal
Volume
34
Published Date
Start Page
1
End Page
1
DOI
10.1096/fasebj.2020.34.s1.00674

Export Control: Post-transcriptional Regulation of the COPII Trafficking Pathway.

The coat protein complex II (COPII) mediates forward trafficking of protein and lipid cargoes from the endoplasmic reticulum. COPII is an ancient and essential pathway in all eukaryotes and COPII dysfunction underlies a range of human diseases. Despite this broad significance, major aspects of COPII trafficking remain incompletely understood. For example, while the biochemical features of COPII vesicle formation are relatively well characterized, much less is known about how the COPII system dynamically adjusts its activity to changing physiologic cues or stresses. Recently, post-transcriptional mechanisms have emerged as a major mode of COPII regulation. Here, we review the current literature on how post-transcriptional events, and especially post-translational modifications, govern the COPII pathway.
Authors
Bisnett, BJ; Condon, BM; Lamb, CH; Georgiou, GR; Boyce, M
MLA Citation
Bisnett, Brittany J., et al. “Export Control: Post-transcriptional Regulation of the COPII Trafficking Pathway.Frontiers in Cell and Developmental Biology, vol. 8, Jan. 2020, p. 618652. Epmc, doi:10.3389/fcell.2020.618652.
URI
https://scholars.duke.edu/individual/pub1474257
PMID
33511128
Source
epmc
Published In
Frontiers in Cell and Developmental Biology
Volume
8
Published Date
Start Page
618652
DOI
10.3389/fcell.2020.618652

Parallel Glyco-SPOT Synthesis of Glycopeptide Libraries.

Glycan recognition is typically studied using free glycans, but glycopeptide presentations represent more physiological conditions for glycoproteins. To facilitate studies of glycopeptide recognition, we developed Glyco-SPOT synthesis, which enables the parallel production of diverse glycopeptide libraries at microgram scales. The method uses a closed system for prolonged reactions required for coupling Fmoc-protected glycoamino acids, including O-, N-, and S-linked glycosides, and release conditions to prevent side reactions. To optimize reaction conditions and sample reaction progress, we devised a biopsy testing method. We demonstrate the efficient utilization of such microscale glycopeptide libraries to determine the specificity of glycan-recognizing antibodies (e.g., CTD110.6) using microarrays, enzyme specificity on-array and in-solution (e.g., ST6GalNAc1, GCNT1, and T-synthase), and binding kinetics using fluorescence polarization. We demonstrated that the glycosylation on these peptides can be expanded using glycosyltransferases both in-solution and on-array. This technology will promote the discovery of biological functions of peptide modifications by glycans.
Authors
Mehta, AY; Veeraiah, RKH; Dutta, S; Goth, CK; Hanes, MS; Gao, C; Stavenhagen, K; Kardish, R; Matsumoto, Y; Heimburg-Molinaro, J; Boyce, M; Pohl, NLB; Cummings, RD
MLA Citation
Mehta, Akul Y., et al. “Parallel Glyco-SPOT Synthesis of Glycopeptide Libraries.Cell Chem Biol, vol. 27, no. 9, Sept. 2020, pp. 1207-1219.e9. Pubmed, doi:10.1016/j.chembiol.2020.06.007.
URI
https://scholars.duke.edu/individual/pub1452832
PMID
32610041
Source
pubmed
Published In
Cell Chem Biol
Volume
27
Published Date
Start Page
1207
End Page
1219.e9
DOI
10.1016/j.chembiol.2020.06.007