O-Mannose Glycans & Muscular Dystrophy
Glycoslytransferases That Control Cell Growth & Differentiation
Roles for Glycans in Notch Signaling
Regulation of Gene Expression by O-GlcNAc
For more details, go to the ASBMB Meeting 2013 program page
and click to expland “Glycobiology.”
A large body of evidence has demonstrated that post-translational modification of proteins by individual sugars or glycans composed of many sugars modulates key properties of glycoproteins. No post-translational modification is better suited for increasing functional diversity of proteins than glycosylation. During this program, the focus will be on how the nontemplate-driven addition of sugars to key proteins plays a critical regulatory role in modulating mammalian signal transduction and how aberrant glycosylation causes a variety of developmental diseases and promotes cancer progression.
The first session will concentrate on how defects in the O-mannose glycosylation pathway are the underlying cause of multiple forms of muscular dystrophy. The O-mannose glycans on dystroglycan are essential for interactions of the cell with the extracellular matrix, and the pathophysiology of congenital muscular dystrophy can be attributed directly to enzymes and proteins that participate in the O-mannosylation pathway.
The second session will discuss glycans that regulate T-cell differentiation, cancer progression and spermatogenesis. These talks will illustrate the key roles that various classes of glycoproteins play in modulating both normal and disease-related signaling and differentiation.
The third session will center on the glycans of a single glycoprotein, Notch, and explore critical roles that various sugars play in Notch signaling pathways. Glycans on Notch modulate ligand binding and Notch activation. This session will focus on this one glycoprotein as a model for how glycosylation can increase functional diversity of proteins.
The final session will move inside the cell and focus on the nucleocytoplasmic O-GlcNAc transferase, functions for O-GlcNAc in CREB-mediated regulation of transcription in long-term memory, and the control of metabolism during oncogenic signaling via O-GlcNAc. These talks, focused on a single sugar modification of nuclear and cytosolic proteins, will illustrate the wide variety of protein functions that can be modulated by nontemplate-driven glycosylation.
Pamela Stanley (email@example.com) is the Horace W. Goldsmith professor of cell biology at the Albert Einstein College of Medicine. Lance Wells (firstname.lastname@example.org) is the Georgia Research Alliance Lars G. Ljungdahl distinguished investigator and an associate professor at the University of Georgia.