| First Author | Delto CF | Year | 2015 |
| Journal | Structure | Volume | 23 |
| Issue | 2 | Pages | 364-73 |
| PubMed ID | 25579817 | Mgi Jnum | J:247418 |
| Mgi Id | MGI:5926673 | Doi | 10.1016/j.str.2014.11.016 |
| Citation | Delto CF, et al. (2015) The LisH motif of muskelin is crucial for oligomerization and governs intracellular localization. Structure 23(2):364-73 |
| abstractText | Neurons regulate the number of surface receptors by balancing the transport to and from the plasma membrane to adjust their signaling properties. The protein muskelin was recently identified as a key factor guiding the transport of alpha1 subunit-containing GABAA receptors. Here we present the crystal structure of muskelin, comprising its N-terminal discoidin domain and Lis1-homology (LisH) motif. The molecule crystallized as a dimer with the LisH motif exclusively mediating oligomerization. Our subsequent biochemical analyses confirmed that the LisH motif acts as a dimerization element in muskelin. Together with an intermolecular head-to-tail interaction, the LisH-dependent dimerization is required to assemble a muskelin tetramer. Intriguingly, our cellular studies revealed that the loss of this dimerization results in a complete redistribution of muskelin from the cytoplasm to the nucleus and impairs muskelin's function in GABAA receptor transport. These studies demonstrate that the LisH-dependent dimerization is a crucial factor for muskelin function. |
