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. 2016 Jan 11;3:86. doi: 10.3389/fcell.2015.00086

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Copyright © 2016 Witkos and Lowe.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Topology and membrane attachment of golgins. Golgins are comprised predominantly of coiled-coil regions (depicted by black helices; note that the frequent short breaks found within the coiled-coil regions of golgins are not shown for simplicity). Golgins can either be directly anchored to the Golgi membrane through carboxy-terminal transmembrane domains (giantin, golgin-84 and CASP), or they can associate with the Golgi membrane through interactions with other Golgi-localized proteins. The carboxy-terminus of GM130 acts as a ligand for the PDZ domains of GRASP65. Trans-Golgi golgins have a GRIP domain that interacts with Arl1, whereas GMAP-210 has an analogous GRAB domain that binds to Arf1. TMF and golgin-160 are attached to the Golgi membrane via binding of their carboxy-terminal regions to Rab6 or Arf1 respectively.