Bicaudal-D regulates COPI-independent Golgi-ER transport by recruiting the dynein-dynactin motor complex

被引:308
作者
Matanis, T
Akhmanova, A
Wulf, P
Del Nery, E
Weide, T
Stepanova, T
Galjart, N
Grosveld, F
Goud, B
De Zeeuw, CI
Barnekow, A
Hoogenraad, CC
机构
[1] Univ Munster, Dept Expt Tumorbiol, D-48149 Munster, Germany
[2] Erasmus Univ, Dept Neurosci, NL-3000 DR Rotterdam, Netherlands
[3] Erasmus Univ, Dept Cell Biol & Genet, NL-3000 DR Rotterdam, Netherlands
[4] Inst Curie, CNRS, UMR 144, F-75248 Paris 05, France
关键词
D O I
10.1038/ncb891
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
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 pathway(1-6). 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-D7-10. 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.
引用
收藏
页码:986 / 992
页数:7
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