We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Actin and Arf1-dependent recruitment of a cortactin-dynamin complex to the Golgi regulates post-Golgi transport.
- Authors
Cao, Hong; Weller, Shaun; Orth, James D.; Chen, Jing; Huang, Bing; Chen, Ji-Long; Stamnes, Mark; McNiven, Mark A.
- Abstract
Cortactin is an actin-binding protein that has recently been implicated in endocytosis. It binds directly to dynamin-2 (Dyn2), a large GTPase that mediates the formation of vesicles from the plasma membrane and the Golgi. Here we show that cortactin associates with the Golgi to regulate the actin- and Dyn2-dependent transport of cargo. Cortactin antibodies stain the Golgi apparatus, labelling peripheral buds and vesicles that are associated with the cisternae. Notably, in vitro or intact-cell experiments show that activation of Arf1 mediates the recruitment of actin, cortactin and Dyn2 to Golgi membranes. Furthermore, selective disruption of the cortactin-Dyn2 interaction significantly reduces the levels of Dyn2 at the Golgi and blocks the transit of nascent proteins from the trans-Golgi network, resulting in swollen and distended cisternae. These findings support the idea of an Arf1-activated recruitment of an actin, cortactin and Dyn2 complex that is essential for Golgi function.
- Subjects
ACTIN; ENDOCYTOSIS; CELL membranes; CARRIER proteins; IMMUNOGLOBULINS; BIOMOLECULES
- Publication
Nature Cell Biology, 2005, Vol 7, Issue 5, p483
- ISSN
1465-7392
- Publication type
Article
- DOI
10.1038/ncb1246