4OYU: Crystal structure of the N-terminal domains of muskelin

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.
PDB ID: 4OYUDownload
MMDB ID: 126838
PDB Deposition Date: 2014/2/13
Updated in MMDB: 2018/07
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 4OYU: dimeric; determined by author and by software (PISA)
Molecular Components in 4OYU
Label Count Molecule
Proteins (2 molecules)
Muskelin(Gene symbol: Mkln1)
Molecule annotation
Chemicals (25 molecules)
Molecule information is not avaliable.
* Click molecule labels to explore molecular sequence information.

Citing MMDB