Rab and actomyosin-dependent fission of transport vesicles at the Golgi complex

The non-processive motor, myosin II, is shown to be an effector of the Golgi-associated Rab6 GTPase. The acto-myosin machinery is involved in the fission of transport carriers from Golgi membranes. Trafficking between membrane compartments is a characteristic of eukaryotic cells and relies on transp...

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Bibliographic Details
Published in:	Nature cell biology Vol. 12; no. 7; pp. 645 - 654
Main Authors:	Goud, B, Miserey-Lenkei, S, Chalancon, G, Echard, A, Bardin, S, Formstecher, E
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 01-07-2010 Nature Publishing Group
Subjects:	631/45/612/1227 631/80/313 631/80/642/1525 Actins - metabolism Actomyosin - metabolism Biological transport Biological Transport - physiology Biomedical and Life Sciences Biosynthesis Cancer Research Cell Biology Cell division Developmental Biology Golgi apparatus Golgi Apparatus - metabolism Guanosine triphosphatase HeLa Cells Humans Intracellular Membranes - metabolism Life Sciences Membranes Models, Biological Myosin Myosin Type II - metabolism Physiological aspects Proteins rab GTP-Binding Proteins - metabolism Signal Transduction - physiology Stem Cells Trafficking France
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Summary:	The non-processive motor, myosin II, is shown to be an effector of the Golgi-associated Rab6 GTPase. The acto-myosin machinery is involved in the fission of transport carriers from Golgi membranes. Trafficking between membrane compartments is a characteristic of eukaryotic cells and relies on transport carriers that bud and fission from a donor membrane, before being transported and fusing with the correct acceptor compartment. Rab GTPases ensure specificity and directionality of trafficking steps by regulating the movement of transport carriers along cytoskeletal tracks, and the recruitment of tethering factors required for the docking and fusion processes. Here we show that Rab6, a Golgi-associated Rab, forms a complex with myosin II, contributes to its localization at the Golgi complex and, unexpectedly, controls the fission of Rab6 vesicles. Inhibition of either Rab6 or myosin II function impairs both the fission of Rab6 transport carriers from Golgi membranes and the trafficking of anterograde and retrograde cargo from the Golgi. These effects are consistent with myosin II being an effector of Rab6 in these processes. Our results provide evidence that the actomyosin system is required in vesicle biogenesis at the Golgi, and uncover a function for Rab GTPases in vesicle fission.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	1465-7392 1476-4679
DOI:	10.1038/ncb2067