Journal
ACS CHEMICAL BIOLOGY
Volume 16, Issue 10, Pages 1994-2003Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.1c00313
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Funding
- NIH K99/R00 Pathway to Independence Award [R00HD090292]
- NIGMS [R35GM142462]
- Skaggs Graduate Fellowship
- Joe W. & Dorothy Dorsett Brown Foundation
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Galectin-1 is a key protein in promoting myogenic differentiation, but the glycoprotein interactors of galectin-1 are not fully understood. A proximity tagging strategy has been used to capture and identify the glycan-mediated glycoprotein interactors of galectin-1 in myoblasts, providing valuable resources for studying the mechanisms through which galectin-1 promotes myogenic differentiation.
Myogenic differentiation, the irreversible developmental process where precursor myoblast muscle stem cells become contractile myotubes, is heavily regulated by glycosylation and glycan-protein interactions at the cell surface and the extracellular matrix. The glycan-binding protein galectin-1 has been found to be a potent activator of myogenic differentiation. While it is being explored as a potential therapeutic for muscle repair, a precise understanding of its glycoprotein interactors is lacking. These gaps are due in part to the difficulties of capturing glycan-protein interactions in live cells. Here, we demonstrate the use of a proximity tagging strategy coupled with quantitative massspectrometry-based proteomics to capture, enrich, and identify the glycan-mediated glycoprotein interactors of galectin-1 in cultured live mouse myoblasts. Our interactome dataset can serve as a resource to aid the determination of mechanisms through which galectin-1 promotes myogenic differentiation. Moreover, it can also facilitate the determination of the physiological glycoprotein counter-receptors of galectin-1. Indeed, we identify several known and novel glycan-mediated ligands of galectin-1 as well as validate that galectin-1 binds the native CD44 glycoprotein in a glycan-mediated manner.
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