ArticleProceedings of the National Academy of Sciences of the United States of America2013
Quantitative analysis of intra-Golgi transport shows intercisternal exchange for all cargo.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Morphological determinants of glycosylation efficiency in Golgi cisternae.PLoS computational biology · 2026Article
- Sorting of secretory proteins at theeLife · 2024Article
- Theoretical approaches for understanding the self-organized formation of the Golgi apparatus.Development, growth & differentiation · 2023Review
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- A novel combinatorial approach of quantitative microscopy and in silico modeling deciphers Arf1-dependent Golgi size regulation.The European physical journal. E, Soft matter · 2019Article
- Stochastic Model of Maturation and Vesicular Exchange in Cellular Organelles.Biophysical journal · 2018Article
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- Nonequilibrium description of de novo biogenesis and transport through Golgi-like cisternae.Scientific reports · 2016Article
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- The Abl/enabled signaling pathway regulates Golgi architecture in Drosophila photoreceptor neurons.Molecular biology of the cell · 2014Article
- Golgi compartmentation and identity.Current opinion in cell biology · 2014Review
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Authors and funding
3 authors.
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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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