JCB logo
Accuri Cytometers
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online 18 April 2005. doi:10.1083/jcb.200501162
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 169, Number 2, 285-295
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 3151K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sahlender, D. A.
Right arrow Articles by Buss, F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sahlender, D. A.
Right arrow Articles by Buss, F.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
*HomoloGene*UniGene
*Substance via MeSH
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis



Daniela A. Sahlender1, Rhys C. Roberts2, Susan D. Arden1, Giulietta Spudich2, Marcus J. Taylor1, J. Paul Luzio1, John Kendrick-Jones2, and Folma Buss1

1 Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, England, UK
2 MRC Laboratory of Molecular Biology, Cambridge CB2 2QH, England, UK

Correspondence to Folma Buss:fb1{at}mole.bio.cam.ac.uk

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.

D.A. Sahlender and R.C. Roberts contributed equally to this work.

Abbreviations used in this paper: MTOC, microtubule organizing center; NRK, normal rat kidney; SEAP, soluble secreted form of the alkaline phosphatase; siRNA, small interfering RNA; VSV-G, vesicular stomatitis virus G-protein.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents