This web page was produced as an assignment for Genetics 677, an undergraduate course at UW-Madison.
A Review of SH3 Domains from a Subset of BAR Proteins Define a UbI-Binding Domain and Implicate Parkin in Synaptic Ubiquitination
The paper SH3 Domains from a Subset of BAR Proteins Define a UbI-Binding Domain and Implicate Parkin in Synaptic Ubiquitination is a study done by Edward Fon’s laboratory at McGill University. The paper characterizes the interaction between the parkin protein and endophilin-A, specifically looking at the domains involved in the process. Parkin, thought to play a role in the ubiquitination of proteins, contains an N-terminal ubiquitin-like domain (UbI). The paper reports that the UbI region of parkin binds SH3 domains of endophilin-A with an affinity similar to proline-rich domains. It was also found that the C-terminal extension of parkin’s UbI domain binds to endophilin-A1 SH3 domain. Additionally, they found this C-terminus interaction to be critical for binding with the SH3 domain. Lastly, they report that phosphorylation can enhance parkin-endophilin-A interactions and possibly regulate their ubiquitination in nerve cells. The finding concludes with the theory that mutated parkin genes will inhibit synaptic transmission and thus lead to recessive Parkinson’s Disease.
| parkin_journal.pdf |
References
1. Trempe, J., Chen, C., Grenier, K., Camacho, E., Kozlov, G., McPherson, P., Gehring, K., and Fon, E. (2009). SH3 Domains from a Subset of BAR Proteins Define a UbI-Binding Domain and Implicate Parkin in Synaptic Ubiquitination. Mol Cell, 36 (6), 1034-47.
