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

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

Standard

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

Harvard

Al-Jubair, T, Steffen, JH, Missel, JW, Kitchen, P, Salman, MM, Bill, RM, Gourdon, P & Törnroth-Horsefield, S 2022, 'Characterization of human aquaporin protein-protein interactions using microscale thermophoresis (MST)', STAR Protocols, vol. 3, no. 2, 101316. https://doi.org/10.1016/j.xpro.2022.101316

APA

Al-Jubair, T., Steffen, J. H., Missel, J. W., Kitchen, P., Salman, M. M., Bill, R. M., Gourdon, P., & Törnroth-Horsefield, S. (2022). Characterization of human aquaporin protein-protein interactions using microscale thermophoresis (MST). STAR Protocols, 3(2), [101316]. https://doi.org/10.1016/j.xpro.2022.101316

Vancouver

Al-Jubair T, Steffen JH, Missel JW, Kitchen P, Salman MM, Bill RM et al. Characterization of human aquaporin protein-protein interactions using microscale thermophoresis (MST). STAR Protocols. 2022;3(2). 101316. https://doi.org/10.1016/j.xpro.2022.101316

Author

Al-Jubair, Tamim ; Steffen, Jonas Hyld ; Missel, Julie Winkel ; Kitchen, Philip ; Salman, Mootaz M. ; Bill, Roslyn M. ; Gourdon, Pontus ; Törnroth-Horsefield, Susanna. / Characterization of human aquaporin protein-protein interactions using microscale thermophoresis (MST). In: STAR Protocols. 2022 ; Vol. 3, No. 2.

Bibtex

@article{9003ac22fbf54e1ab7e168e863166e31,
title = "Characterization of human aquaporin protein-protein interactions using microscale thermophoresis (MST)",
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).",
keywords = "Cell Membrane, Protein Biochemistry, Single-molecule Assays",
author = "Tamim Al-Jubair and Steffen, {Jonas Hyld} and Missel, {Julie Winkel} and Philip Kitchen and Salman, {Mootaz M.} and Bill, {Roslyn M.} and Pontus Gourdon and Susanna T{\"o}rnroth-Horsefield",
note = "Publisher Copyright: {\textcopyright} 2022 The Authors",
year = "2022",
doi = "10.1016/j.xpro.2022.101316",
language = "English",
volume = "3",
journal = "STAR Protocols",
issn = "2666-1667",
publisher = "Cell Press",
number = "2",

}

RIS

TY - JOUR

T1 - Characterization of human aquaporin protein-protein interactions using microscale thermophoresis (MST)

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

N1 - Publisher Copyright: © 2022 The Authors

PY - 2022

Y1 - 2022

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

UR - http://www.scopus.com/inward/record.url?scp=85128271354&partnerID=8YFLogxK

U2 - 10.1016/j.xpro.2022.101316

DO - 10.1016/j.xpro.2022.101316

M3 - Journal article

C2 - 35479114

AN - SCOPUS:85128271354

VL - 3

JO - STAR Protocols

JF - STAR Protocols

SN - 2666-1667

IS - 2

M1 - 101316

ER -

ID: 311125776