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Optineurin Links Myosin VI to the Golgi Complex and is Involved in Golgi Organization and Exocytosis

Overview
Journal J Cell Biol
Specialty Cell Biology
Date 2005 Apr 20
PMID 15837803
Citations 192
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Abstract

Myosin VI plays a role in the maintenance of Golgi morphology and in exocytosis. In a yeast 2-hybrid screen we identified optineurin as a binding partner for myosin VI at the Golgi complex and confirmed this interaction in a range of protein interaction studies. Both proteins colocalize at the Golgi complex and in vesicles at the plasma membrane. When optineurin is depleted from cells using RNA interference, myosin VI is lost from the Golgi complex, the Golgi is fragmented and exocytosis of vesicular stomatitis virus G-protein to the plasma membrane is dramatically reduced. Two further binding partners for optineurin have been identified: huntingtin and Rab8. We show that myosin VI and Rab8 colocalize around the Golgi complex and in vesicles at the plasma membrane and overexpression of constitutively active Rab8-Q67L recruits myosin VI onto Rab8-positive structures. These results show that optineurin links myosin VI to the Golgi complex and plays a central role in Golgi ribbon formation and exocytosis.

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References
1.
Gill S, Schroer T, Szilak I, Steuer E, Sheetz M, Cleveland D . Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein. J Cell Biol. 1991; 115(6):1639-50. PMC: 2289205. DOI: 10.1083/jcb.115.6.1639. View

2.
Buss F, Luzio J, Kendrick-Jones J . Myosin VI, a new force in clathrin mediated endocytosis. FEBS Lett. 2001; 508(3):295-9. DOI: 10.1016/s0014-5793(01)03065-4. View

3.
Pepperkok R, Scheel J, Horstmann H, Hauri H, Griffiths G, Kreis T . Beta-COP is essential for biosynthetic membrane transport from the endoplasmic reticulum to the Golgi complex in vivo. Cell. 1993; 74(1):71-82. DOI: 10.1016/0092-8674(93)90295-2. View

4.
Huber L, Pimplikar S, Parton R, Virta H, Zerial M, Simons K . Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane. J Cell Biol. 1993; 123(1):35-45. PMC: 2119815. DOI: 10.1083/jcb.123.1.35. View

5.
Huber L, de Hoop M, Dupree P, Zerial M, Simons K, Dotti C . Protein transport to the dendritic plasma membrane of cultured neurons is regulated by rab8p. J Cell Biol. 1993; 123(1):47-55. PMC: 2119825. DOI: 10.1083/jcb.123.1.47. View