Brief Communication abstract
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 complex
Theodoros 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. Hoogenraad2,6
The 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.
- Department of Experimental Tumorbiology, University of Muenster, Badestrasse 9, D-48149 Muenster, Germany
- Department of Neuroscience, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands
- Department of Cell Biology and Genetics, Erasmus University Rotterdam, P.O. Box 1738, 3000 DR Rotterdam, The Netherlands
- UMR CNRS 144, Institut Curie, 26 rue d'Ulm, 75248 Paris Cedex 05, France
- These authors contributed equally to this work
- Current address: Picower Center for Learning and Memory, Massachusetts Institute of Technology, 77 Massachusetts Avenue (E18-215), Cambridge MA 02139, USA
Correspondence to: Casper C. Hoogenraad2,6 e-mail: hoogenra@mit.edu
Correspondence to: Anna Akhmanova3,5 e-mail: anna.akhmanova@chello.nl
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