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Published 10 December 2001. doi:10.1083/jcb.200108079
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© The Rockefeller University Press, 0021-9525/2001/12/877 $5.00
The Journal of Cell Biology, Volume 155, Number 6, December 10, 2001 877-884


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A GRASP55-rab2 effector complex linking Golgi structure to membrane traffic

Benjamin Short1,2, Christian Preisinger1, Roman Körner1, Robert Kopajtich1, Olwyn Byron2 and Francis A. Barr1

1 Department of Cell Biology, Max-Planck-Institute of Biochemistry, Martinsried D-82152, Germany
2 Division of Infection and Immunity, Faculty of Biomedical and Life Science, University of Glasgow, Glasgow, UK

Address correspondence to Francis Barr, Max-Planck-Institute of Biochemistry, Dept. of Cell Biology, Am Klopferspitz 18a, Martinsried D-85152, Germany. Tel.: 49-89-8578-3135. Fax: 49-89-8578-3102. E-mail: barr{at}biochem.mpg.de

Membrane traffic between the endoplasmic reticulum (ER) and Golgi apparatus and through the Golgi apparatus is a highly regulated process controlled by members of the rab GTPase family. The GTP form of rab1 regulates ER to Golgi transport by interaction with the vesicle tethering factor p115 and the cis-Golgi matrix protein GM130, also part of a complex with GRASP65 important for the organization of cis-Golgi cisternae. Here, we find that a novel coiled-coil protein golgin-45 interacts with the medial-Golgi matrix protein GRASP55 and the GTP form of rab2 but not other Golgi rab proteins. Depletion of golgin-45 disrupts the Golgi apparatus and causes a block in secretory protein transport. These results demonstrate that GRASP55 and golgin-45 form a rab2 effector complex on medial-Golgi essential for normal protein transport and Golgi structure.

Key Words: Golgi apparatus; protein transport; rab GTPases; rab2; Golgi stacks


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