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Michael Boyce

Assistant Professor of Biochemistry
(919) 684-9906
Research Interest: 
Membranes and organelles
Signal transduction
Research Summary: 
Cell signaling through protein glycosylation, using chemical, biochemical and cell biological methods.
Research Description: 

The long-term goal of the Boyce lab is to understand the role of protein glycosylation in mammalian cell signaling and physiology. Protein glycosylation is the most abundant post-translational modification in nature and, as a sugar-based modification, it lies at the nexus of cell signaling and cell metabolism. However, because glycosylation is a dynamic and non-templated process, it can be difficult to study using conventional biological techniques alone. Our lab uses a range of biochemical, cell and chemical biological methods to dissect the role of protein glycosylation in mammals. Specifically, we focus on two distinct forms of glycosylation. First, we aim to understand how the dynamic signaling by ß-N-acetylglucosamine on intracellular proteins senses and regulates cell metabolism. Second, we aim to understand how the quality control machinery in the ER and Golgi senses mis-glycosylated proteins in the secretory pathway, and how the cell copes with this form of stress in health and disease.

A chemical glycoproteomics platform reveals O-GlcNAcylation of mitochondrial voltage-dependent anion channel 2.
Palaniappan KK, Hangauer MJ, Smith TJ, Smart BP, Pitcher AA, Cheng EH, Bertozzi CR, Boyce M.
Cell Rep. 2013. 5:546-52.

Metabolic cross-talk allows labeling of O-linked beta-N-acetylglucosamine-modified proteins via the N-acetylgalactosamine salvage pathway.
Boyce M, Carrico IS, Ganguli AS, Yu SH, Hangauer MJ, Hubbard SC, Kohler JJ, Bertozzi CR.
Proc Natl Acad Sci U S A. 2011. 108:3141-6.

Bringing chemistry to life.
Boyce M, Bertozzi CR.
Nat Methods. 2011. 8:638-42.

Metabolic labeling enables selective photocrosslinking of O-GlcNAc-modified proteins to their binding partners.
Yu SH, Boyce M, Wands AM, Bond MR, Bertozzi CR, Kohler JJ.
Proc Natl Acad Sci U S A. 2012. 109:4834-9.

A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress.
Boyce M, Bryant KF, Jousse C, Long K, Harding HP, Scheuner D, Kaufman RJ, Ma D, Coen DM, Ron D, Yuan J.
Science. 2005. 307:935-9.