Impact of Golgi dynamics and Golgi morphology on the regulation of glycosylation
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Updated: May 11, 2026

Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
Published on: December 26, 2011
1The Department of Biochemistry and Pharmacology, Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Parkville, VIC 3010, Australia.
Abstract:
The Golgi apparatus is a highly dynamic organelle and central to the regulation of protein glycosylation, cargo sorting and additional cellular processes such as mitosis, stress responses, autophagy and inflammation. There have been major advances in understanding the dynamics of the Golgi apparatus and the relationship between remodelling the Golgi architecture and function. Membrane structural/scaffold proteins of the Golgi, including golgins, GRASPs and adaptors interact with a diverse range of cytoskeletal and signalling molecules and play a major role in the regulation of the Golgi morphology and function. Modulation of the higher-order Golgi ribbon architecture in mammalian cells is directly associated with physiological and pathological responses, including neurological diseases and cancer. An important question is the influence of morphological states of the Golgi architecture on the fine tuning of glycosylation. Here we review the relationship between the morphology and function of this organelle, in physiology and disease, especially to in relation to the impact of the fragmentation of the Golgi ribbon on the steady state location of glycosyltransferases and glycan synthesis. The current unresolved issues relevant to changes in Golgi morphology on protein glycosylation are highlighted.
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