The LisH Motif of Muskelin Is Crucial for Oligomerization and Governs Intracellular Localization

Carolyn F Delto; Frank F Heisler; Jochen Kuper; Bodo Sander; Matthias Kneussel; Hermann Schindelin

doi:10.1016/j.str.2014.11.016

The LisH Motif of Muskelin Is Crucial for Oligomerization and Governs Intracellular Localization

Standard

The LisH Motif of Muskelin Is Crucial for Oligomerization and Governs Intracellular Localization. / Delto, Carolyn F; Heisler, Frank F; Kuper, Jochen; Sander, Bodo; Kneussel, Matthias; Schindelin, Hermann.

in: STRUCTURE, Jahrgang 23, Nr. 2, 03.02.2015, S. 364-73.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Delto, CF, Heisler, FF, Kuper, J, Sander, B, Kneussel, M & Schindelin, H 2015, 'The LisH Motif of Muskelin Is Crucial for Oligomerization and Governs Intracellular Localization', STRUCTURE, Jg. 23, Nr. 2, S. 364-73. https://doi.org/10.1016/j.str.2014.11.016

APA

Delto, C. F., Heisler, F. F., Kuper, J., Sander, B., Kneussel, M., & Schindelin, H. (2015). The LisH Motif of Muskelin Is Crucial for Oligomerization and Governs Intracellular Localization. STRUCTURE, 23(2), 364-73. https://doi.org/10.1016/j.str.2014.11.016

Vancouver

Delto CF, Heisler FF, Kuper J, Sander B, Kneussel M, Schindelin H. The LisH Motif of Muskelin Is Crucial for Oligomerization and Governs Intracellular Localization. STRUCTURE. 2015 Feb 3;23(2):364-73. https://doi.org/10.1016/j.str.2014.11.016

Bibtex

@article{625f20b0c3bf4a9a90d89825b9d9ec04,

title = "The LisH Motif of Muskelin Is Crucial for Oligomerization and Governs Intracellular Localization",

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.",

author = "Delto, {Carolyn F} and Heisler, {Frank F} and Jochen Kuper and Bodo Sander and Matthias Kneussel and Hermann Schindelin",

year = "2015",

month = feb,

day = "3",

doi = "10.1016/j.str.2014.11.016",

language = "English",

volume = "23",

pages = "364--73",

journal = "STRUCTURE",

issn = "0969-2126",

publisher = "Cell Press",

number = "2",

}

RIS

TY - JOUR

T1 - The LisH Motif of Muskelin Is Crucial for Oligomerization and Governs Intracellular Localization

AU - Delto, Carolyn F

AU - Heisler, Frank F

AU - Kuper, Jochen

AU - Sander, Bodo

AU - Kneussel, Matthias

AU - Schindelin, Hermann

PY - 2015/2/3

Y1 - 2015/2/3

N2 - 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.

AB - 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.

U2 - 10.1016/j.str.2014.11.016

DO - 10.1016/j.str.2014.11.016

M3 - SCORING: Journal article

C2 - 25579817

VL - 23

SP - 364

EP - 373

JO - STRUCTURE

JF - STRUCTURE

SN - 0969-2126

IS - 2

ER -