Nature Cell Biology
4, 986 - 992 (2002)
Published online: 25 November 2002; | doi:10.1038/ncb891
There is an Erratum (January 2003) associated with this Brief Communication.
Bicaudal-D regulates COPI-independent Golgi−ER transport by recruiting the dynein−dynactin motor complexTheodoros Matanis1, 5, Anna Akhmanova3, 5, Phebe Wulf2, Elaine Del Nery4, Thomas Weide1, Tatiana Stepanova3, Niels Galjart3, Frank Grosveld3, Bruno Goud4, Chris I. De Zeeuw2, Angelika Barnekow1
& Casper C. Hoogenraad2, 61
Department of Experimental Tumorbiology, University of Muenster, Badestrasse 9, D-48149 Muenster, Germany
2
Department of Neuroscience, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands
3
Department of Cell Biology and Genetics, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands
4
UMR CNRS 144, Institut Curie, 26 rue d'Ulm, 75248 Paris Cedex 05, France
5
These authors contributed equally to this work 6
Current address: Picower Center for Learning and Memory, Massachusetts Institute of Technology, 77 Massachusetts Avenue (E18-215), Cambridge MA 02139, USA
Correspondence should be addressed to Casper C. Hoogenraad hoogenra@mit.edu or Anna Akhmanova anna.akhmanova@chello.nlThe small GTPase Rab6a is involved in the regulation of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) in a coat complex coatomer protein I (COPI)-independent pathway1,
2,
3,
4,
5,
6. Here, we used a yeast two-hybrid approach to identify binding partners of Rab6a. In particular, we identified the dynein−dynactin-binding protein Bicaudal-D1 (BICD1), one of the two mammalian homologues of Drosophila Bicaudal-D7,
8,
9,
10. BICD1 and BICD2 colocalize with Rab6a on the trans-Golgi network (TGN) and on cytoplasmic vesicles, and associate with Golgi membranes in a Rab6-dependent manner. Overexpression of BICD1 enhances the recruitment of dynein−dynactin to Rab6a-containing vesicles. Conversely, overexpression of the carboxy-terminal domain of BICD, which can interact with Rab6a but not with cytoplasmic dynein, inhibits microtubule minus-end-directed movement of green fluorescent protein (GFP)−Rab6a vesicles and induces an accumulation of Rab6a and COPI-independent ER cargo in peripheral structures. These data suggest that coordinated action between Rab6a, BICD and the dynein−dynactin complex controls COPI-independent Golgi−ER transport.
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