Invited Symposium: Intracellular Traffic of Organelles
Yamabhai, M. (Department of Pharmacology, University of Wisconsin, USA)
Ramjaun, AR (Department of Neurology & Neurosurgery, Montreal Neurological Institute, McGill University, Canada)
Kay, BK (Department of Pharmacology, University of Wisconsin, USA)
McPherson, PS (Department of Neurology & Neurosurgery, Montreal Neurological Institute, McGill University, USA)
Src homology 3 (SH3) and Eps15 homology (EH) domains are protein modules mediating protein-protein interactions in a variety of cellular processes including endocytosis. A link between these domains has been provided with the identification of intersectin, a novel protein which we cloned through a screen of an expression library with a src SH3 domain peptide ligand. Intersectin is 1,270 amino acids long and contains two N-terminal EH domains, a central helix forming region, and five C-terminal SH3 domains. Through its SH3 domains, intersectin interacts with the endocytic proteins dynamin and synaptojanin. We screened a cDNA expression library with the EH domains of intersectin, and identified two the mouse homologue of rat Epsin, an Eps15-binding protein recently implicated in clathrin-mediated endocytosis (Chen et al., Nature, 1998). Both Ibp1 and Ibp2 contain three copies of the EH domain-binding motif asparagine-proline-phenylalanine (NPF). We are currently examining the biochemical and cellular properties of intersectin and its relationship to Ibp1/2 in vivo.
Back to the top.
| Discussion Board | Next Page | Your Symposium |
|Hussain, NK; Yamabhai, M.; Ramjaun, AR; Kay, BK; McPherson, PS; (1998). Intersectin: a Novel Adaptor Protein Functioning in Endocytosis. Presented at INABIS '98 - 5th Internet World Congress on Biomedical Sciences at McMaster University, Canada, Dec 7-16th. Invited Symposium. Available at URL http://www.mcmaster.ca/inabis98/klip/hussain0258/index.html|
|© 1998 Author(s) Hold Copyright|