Characterization of human aquaporin protein-protein interactions using microscale thermophoresis (MST)

Tamim Al-Jubair; Jonas Hyld Steffen; Julie Winkel Missel; Philip Kitchen; Mootaz M. Salman; Roslyn M. Bill; Pontus Gourdon; Susanna Törnroth-Horsefield

doi:10.1016/j.xpro.2022.101316

Characterization of human aquaporin protein-protein interactions using microscale thermophoresis (MST)

Tamim Al-Jubair^*, Jonas Hyld Steffen, Julie Winkel Missel, Philip Kitchen, Mootaz M. Salman, Roslyn M. Bill, Pontus Gourdon, Susanna Törnroth-Horsefield

^*Corresponding author for this work

Molecular Cardiology and Membrane Proteins

Research output: Contribution to journal › Journal article › Research › peer-review

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Abstract

Aquaporin water channels (AQPs) are membrane proteins that maintain cellular water homeostasis. The interactions between human AQPs and other proteins play crucial roles in AQP regulation by both gating and trafficking. Here, we describe a protocol for characterizing the interaction between a human AQP and a soluble interaction partner using microscale thermophoresis (MST). MST has the advantage of low sample consumption and high detergent compatibility enabling AQP protein-protein interaction investigation with a high level of control of components and environment. For complete details on the use and execution of this protocol, please refer to Kitchen et al. (2020) and Roche et al. (2017).

Original language	English
Article number	101316
Journal	STAR Protocols
Volume	3
Issue number	2
Number of pages	8
ISSN	2666-1667
DOIs	https://doi.org/10.1016/j.xpro.2022.101316
Publication status	Published - 2022

Bibliographical note

Publisher Copyright:
© 2022 The Authors

Keywords

Cell Membrane
Protein Biochemistry
Single-molecule Assays

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Characterization of human aquaporin protein-protein interactions using microscale thermophoresis (MST). / Al-Jubair, Tamim; Steffen, Jonas Hyld ; Missel, Julie Winkel; Kitchen, Philip; Salman, Mootaz M.; Bill, Roslyn M.; Gourdon, Pontus; Törnroth-Horsefield, Susanna.

In: STAR Protocols, Vol. 3, No. 2, 101316, 2022.

Research output: Contribution to journal › Journal article › Research › peer-review

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abstract = "Aquaporin water channels (AQPs) are membrane proteins that maintain cellular water homeostasis. The interactions between human AQPs and other proteins play crucial roles in AQP regulation by both gating and trafficking. Here, we describe a protocol for characterizing the interaction between a human AQP and a soluble interaction partner using microscale thermophoresis (MST). MST has the advantage of low sample consumption and high detergent compatibility enabling AQP protein-protein interaction investigation with a high level of control of components and environment. For complete details on the use and execution of this protocol, please refer to Kitchen et al. (2020) and Roche et al. (2017).",

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AU - Al-Jubair, Tamim

AU - Steffen, Jonas Hyld

AU - Missel, Julie Winkel

AU - Kitchen, Philip

AU - Salman, Mootaz M.

AU - Bill, Roslyn M.

AU - Gourdon, Pontus

AU - Törnroth-Horsefield, Susanna

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N2 - Aquaporin water channels (AQPs) are membrane proteins that maintain cellular water homeostasis. The interactions between human AQPs and other proteins play crucial roles in AQP regulation by both gating and trafficking. Here, we describe a protocol for characterizing the interaction between a human AQP and a soluble interaction partner using microscale thermophoresis (MST). MST has the advantage of low sample consumption and high detergent compatibility enabling AQP protein-protein interaction investigation with a high level of control of components and environment. For complete details on the use and execution of this protocol, please refer to Kitchen et al. (2020) and Roche et al. (2017).

AB - Aquaporin water channels (AQPs) are membrane proteins that maintain cellular water homeostasis. The interactions between human AQPs and other proteins play crucial roles in AQP regulation by both gating and trafficking. Here, we describe a protocol for characterizing the interaction between a human AQP and a soluble interaction partner using microscale thermophoresis (MST). MST has the advantage of low sample consumption and high detergent compatibility enabling AQP protein-protein interaction investigation with a high level of control of components and environment. For complete details on the use and execution of this protocol, please refer to Kitchen et al. (2020) and Roche et al. (2017).

KW - Cell Membrane

KW - Protein Biochemistry

KW - Single-molecule Assays

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DO - 10.1016/j.xpro.2022.101316

M3 - Journal article

C2 - 35479114

AN - SCOPUS:85128271354

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JO - STAR Protocols

JF - STAR Protocols

SN - 2666-1667

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ER -

Characterization of human aquaporin protein-protein interactions using microscale thermophoresis (MST)

Abstract

Bibliographical note

Keywords

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