New paper by the Aebi Lab:

Analysis of site-specific N-glycan remodeling in the endoplasmic reticulum and the Golgi.

by Markus Christian Schlumberger

Ivan Hang, Chia-Wei Lin, Oliver C. Grant, Susanna Fleurkens, Thomas K. Villiger, Miroslav Soos, Massimo Morbidelli, Robert J. Woods, Robert Gauss & Markus Aebi

Glycobiology. 2015 doi: 10.1093/glycob/cwv058

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The hallmark of N-linked protein glycosylation is the generation of diverse glycan structures in the secretory pathway. Dynamic, non-template-driven processes of N-glycan remodeling in the endoplasmic reticulum and the Golgi provide the cellular setting for structural diversity. We applied newly developed mass spectrometry-based analytics to quantify site-specific N-glycan remodeling of the model protein Pdi1p expressed in insect cells. Molecular dynamics simulation, mutational analysis, kinetic studies of in vitro processing events and glycan flux analysis supported the defining role of the protein in N-glycan processing.

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