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Updated: Aug 24, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
Predicting function from structure: 3D structure studies of the mammalian Golgi complex
Soren Mogelsvang1, Brad J Marsh, Mark S Ladinsky
1University of Colorado School of Medicine, Department of Cell and Developmental Biology, University of Colorado Health Sciences Center, Denver, CO 80262, USA.
Abstract:
3D electron tomography studies of the structure of the mammalian Golgi complex have led to four functional predictions (1). The sorting and exit site from the Golgi comprises two or three distinct trans-cisternae (2). The docking of vesicular-tubular clusters at the cis-face and the fragmentation of trans-cisternae are coordinated (3). The mechanisms of transport through, and exit from, the Golgi vary with physiological state, and in different cells and tissues (4). Specialized trans-ER functions in the delivery of ceramide to sphingomyelin synthase in the trans-Golgi membrane, for the regulated sorting via sphingolipid-cholesterol-rich domains. These structure-based predictions can now be tested using a variety of powerful cell and molecular tools.
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