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

Citation:
Abstract
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)
2
Muskelin(Gene symbol: Mkln1)
Molecule annotation
Chemicals (25 molecules)
1
23
2
1
3
1
Molecule information is not avaliable.
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