4OYU

Crystal structure of the N-terminal domains of muskelin

4OYU の概要

• エントリーDOI: 10.2210/pdb4oyu/pdb
• 分子名称: Muskelin, 1,2-ETHANEDIOL, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: discoidin domain, lish motif, dimer, protein binding
• 由来する生物種: Rattus norvegicus (Rat)
• 細胞内の位置: Cytoplasm : Q99PV3
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 47872.83

構造登録者

Delto, C.,Kuper, J.,Schindelin, H. (登録日: 2014-02-13, 公開日: 2015-02-11, 最終更新日: 2023-12-27)

主引用文献

Delto, C.F.,Heisler, F.F.,Kuper, J.,Sander, B.,Kneussel, M.,Schindelin, H.
The LisH Motif of Muskelin Is Crucial for Oligomerization and Governs Intracellular Localization.
Structure, 23:364-373, 2015

PubMed 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 α1 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.

PubMed: 25579817
DOI: 10.1016/j.str.2014.11.016

実験手法

X-RAY DIFFRACTION (1.8 Å)