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Updated: Aug 17, 2026

Quantitative Localization of a Golgi Protein by Imaging Its Center of Fluorescence Mass
Published on: August 10, 2017
Golgins and GTPases, giving identity and structure to the Golgi apparatus
Benjamin Short1, Alexander Haas, Francis A Barr
1Intracellular Protein Transport, Independent Junior Research Group, Max-Planck-Institute of Biochemistry, Martinsried, 82152, Germany.
Abstract:
In this review we will focus on the recent advances in how coiled-coil proteins of the golgin family give identity and structure to the Golgi apparatus in animal cells. A number of recent studies reveal a common theme for the targeting of golgins containing the ARL-binding GRIP domain, and the related ARF-binding GRAB domain. Similarly, other golgins such as the vesicle tethering factor p115 and Bicaudal-D are targeted by the Rab GTPases, Rab1 and Rab6, respectively. Together golgins and their regulatory GTPases form a complex network, commonly known as the Golgi matrix, which organizes Golgi membranes and regulates membrane trafficking.
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