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First published online 14 April 2008
doi: 10.1242/jcs.014324

Journal of Cell Science 121, 1538-1546 (2008)
Published by The Company of Biologists 2008
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Research Article

TbG63, a golgin involved in Golgi architecture in Trypanosoma brucei

Irene Barinaga-Rementeria Ramirez1, Christopher L. de Graffenried2, Ingo Ebersberger3, Jordan Yelinek2, Cynthia Y. He4, Albert Price5 and Graham Warren6,*

1 Faculty of Life Sciences, University of Manchester, The Michael Smith Building, Oxford Road, Manchester, UK
2 Department of Cell Biology, Yale University School of Medicine, New Haven, CT, USA
3 Center for Integrative Bioinformatics Vienna, Max F. Perutz Laboratories, Dr Bohr Gasse 9, A-1030 Vienna, Austria
4 Department of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore 117543
5 VaxInnate, New Haven, CT, USA
6 Max F. Perutz Laboratories, University of Vienna, Medical University of Vienna, Dr Bohr Gasse 9, Vienna, 1030, Austria

* Author for correspondence (e-mail: graham.warren{at}univie.ac.at)

Accepted 7 February 2008

Golgins are coiled-coil proteins that have been implicated in the structure and function of the Golgi complex. Here, we identify and characterize a trypanosomal golgin, TbG63, showing that it has a C-terminal membrane anchor and an N-terminus that projects into the cytoplasm. TbG63 in procyclic parasites is localized to the Golgi and interacts with the active, GTP-form of TbRab1A. Overexpression of TbG63 has dramatic effects on Golgi architecture – effects that require the N-terminus – whereas depletion has little, if any, effect on the growth rate. By contrast, in the bloodstream form of the parasite, depletion of TbG63 slows growth, although it has no obvious effect on the transport of a variant surface glycoprotein (VSG) or on Golgi structure. TbG63 might be a useful tool to study the structure and functioning of the Golgi complex.

Key words: Golgi, Golgin, Trypanosome, Brucei, Architecture, Morphology, Rab, GTPase


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