Abstract

Introduction

Materials & Methods

Results

Discussion & Conclusion

References

Discussion
Board

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.

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Presentation Number SAhussain0258
Keywords: SH3 domain, EH domain, endocytosis, clathrin