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Marra, Pierfrancesco
(2002).
DOI: https://doi.org/10.21954/ou.ro.0000fd3f
Abstract
The Golgi complex represents a crossroad for many intracellular trafficking pathways and is therefore subjected to a continuous flux of membranes. Despite this, the Golgi complex preserves a unique architecture that has been the subject of many investigations. Its organisation is the result of the combined actions of many molecular machineries that are only partially characterised. Cytoskeletal structures, such as the spectrin-based cytoskeleton, and multiprotein complexes, such as the Golgi matrix (a Triton-X-100-resistant complex of proteins), have been suggested to be involved in the generation of the Golgi architecture. Recently, β-spectrin, actin, ankyrin and adducin, components of the spectrin skeleton, have been found to be associated with Golgi membranes in a way that is controlled by a key regulator of the Golgi function: the small GTPase ARF. Spectrin has been functionally implicated in the transport of newly-synthesised proteins from the endoplasmic reticulum (ER) to the Golgi. The role of spectrin as a membrane organiser in other membrane compartments suggests, however, that it may also be involved in the structural organisation of the Golgi complex. The role and possible relationships of the Golgi matrix and the Golgi-associated spectrin skeleton have been investigated in the present study. The results obtained indicate that the spectrin skeleton does indeed participate in the structural organisation of the Golgi complex, and that Golgi matrix proteins undergo recycling through pre-Golgi compartments, and are likely to play an important role in the morphogenesis of ER-derived transport complexes into Golgi cistemae at the cis pole of the Golgi stacks.
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