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. • The relationship between the cell biology of Golgi architecture and regulation of protein glycosylation. • Role of Golgi structural proteins in regulation of Golgi morphology. • Review of different mechanisms by which Golgi morphology influences fine tuning of glycosylation. • Role of cargo adaptors, golgins and GRASPs in regulating localization of glycosyltransferases. • Unresolved issues relevant to impact of Golgi morphology on protein glycosylation.
Paul A. Gleeson (Wed,) studied this question.