Journal article
Actin and Arf1-dependent recruitment of a cortactin-dynamin complex to the Golgi regulates post-Golgi transport
Nature cell biology, Vol.7(5), pp.483-492
05/2005
DOI: 10.1038/ncb1246
PMID: 15821732
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.
Details
- Title: Subtitle
- Actin and Arf1-dependent recruitment of a cortactin-dynamin complex to the Golgi regulates post-Golgi transport
- Creators
- Jing Chen - Center for Basic Research in Digestive Diseases and Department of Biochemistry and Molecular Biology, Mayo ClinicBing Huang - Center for Basic Research in Digestive Diseases and Department of Biochemistry and Molecular Biology, Mayo ClinicJames D Orth - Department of Biochemistry and Molecular Biology, 1642D Guggenheim Building, Mayo ClinicShaun Weller - Center for Basic Research in Digestive Diseases and Department of Biochemistry and Molecular Biology, Mayo ClinicMark A McNiven - Center for Basic Research in Digestive Diseases and Department of Biochemistry and Molecular Biology, Mayo Clinic Department of Biochemistry and Molecular Biology, 1642D Guggenheim Building, Mayo ClinicMark Stamnes - Department of Physiology and Biophysics, University of Iowa College of MedicineHong Cao - Center for Basic Research in Digestive Diseases and Department of Biochemistry and Molecular Biology, Mayo ClinicJi-Long Chen - Department of Physiology and Biophysics, University of Iowa College of Medicine
- Resource Type
- Journal article
- Publication Details
- Nature cell biology, Vol.7(5), pp.483-492
- DOI
- 10.1038/ncb1246
- PMID
- 15821732
- ISSN
- 1465-7392
- eISSN
- 1476-4679
- Language
- English
- Date published
- 05/2005
- Academic Unit
- Molecular Physiology and Biophysics; Internal Medicine
- Record Identifier
- 9984025311602771
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