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Updated: May 8, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
Quantitative analysis of intra-Golgi transport shows intercisternal exchange for all cargo
Serge Dmitrieff1, Madan Rao, Pierre Sens
1Laboratoire Gulliver, Centre National de la Recherche Scientifique-Ecole Supérieure de Physique et de Chimie Industrielles, Unité Mixte de Recherche 7083, 75231 Paris Cedex 05, France.
Abstract:
The mechanisms controlling the transport of proteins through the Golgi stack of mammalian and plant cells is the subject of intense debate, with two models, cisternal progression and intercisternal exchange, emerging as major contenders. A variety of transport experiments have claimed support for each of these models. We reevaluate these experiments using a single quantitative coarse-grained framework of intra-Golgi transport that accounts for both transport models and their many variants. Our analysis makes a definitive case for the existence of intercisternal exchange both for small membrane proteins and large protein complexes--this implies that membrane structures larger than the typical protein-coated vesicles must be involved in transport. Notwithstanding, we find that current observations on protein transport cannot rule out cisternal progression as contributing significantly to the transport process. To discriminate between the different models of intra-Golgi transport, we suggest experiments and an analysis based on our extended theoretical framework that compare the dynamics of transiting and resident proteins.
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