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

Department of Biochemistry and Structural Biology, Lund University, P.O. Box 124, 221 00 Lund, Sweden.
Department of Biomedical Sciences, University of Copenhagen, 2200 Copenhagen, Denmark.
Department of Physiology, Anatomy and Genetics, Kavli Institute for NanoScience Discovery, University of Oxford, Parks Road, OX1 3PT Oxford, UK.; Oxford Parkinson's Disease Centre, University of Oxford, Oxford, UK.
Department of Biomedical Sciences, University of Copenhagen, 2200 Copenhagen, Denmark.; Department of Experimental Medical Science, Lund University, P.O. Box 118, 221 00 Lund, Sweden.

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

149 Downloads (Pure)

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
Early online date	15 Apr 2022
DOIs	https://doi.org/10.1016/j.xpro.2022.101316
Publication status	Published - 17 Jun 2022

Bibliographical note

© 2022 The Authors. This is an open access article under the CC BY license 4.0

Funding Information:
We acknowledge the Swedish Research Council (to S.T.-H. through 2013-05945 and 2019-06106); the Crafoord Foundation (to S.T.-H. through 20140811 and 20180916); the Magnus Bergvall Foundation (to S.T.-H. through 2015-01534); the Knut and Alice Wallenberg Foundation (to P.G. through KAW 2015.0131 and 2020.0194); the Lundbeck Foundation (to P.G. through R133-A12689 and R313-2019-774); The Independent Research Fund Denmark (to P.G. through 4183-00559); NordForsk (to P.G. through 82000); UK Biotechnology & Biosciences Research Council (to R.M.B. and P.K. through BB/P025927/1); P.K. is the recipient of an Aston University 50th Anniversary Prize Fellowship: M.M.S. is supported through funding through funding by Leverhulme Trust (ECF-2021-602 ).

Keywords

Humans
Cell Membrane
Homeostasis
Single-molecule Assays
Proteins - metabolism
Aquaporins - metabolism
Protein Biochemistry
Proteins/metabolism
Aquaporins/metabolism

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10.1016/j.xpro.2022.101316Licence: CC BY 4.0

Characterization of human aquaporin protein-protein interactions
© 2022 The Authors. This is an open access article under the CC BY license 4.0
Final published version, 1.75 MBLicence: CC BY 4.0

Cite this

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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 = "Humans, Cell Membrane, Homeostasis, Single-molecule Assays, Proteins - metabolism, Aquaporins - metabolism, Protein Biochemistry, Proteins/metabolism, Aquaporins/metabolism",

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 = "{\textcopyright} 2022 The Authors. This is an open access article under the CC BY license 4.0 Funding Information: We acknowledge the Swedish Research Council (to S.T.-H. through 2013-05945 and 2019-06106); the Crafoord Foundation (to S.T.-H. through 20140811 and 20180916); the Magnus Bergvall Foundation (to S.T.-H. through 2015-01534); the Knut and Alice Wallenberg Foundation (to P.G. through KAW 2015.0131 and 2020.0194); the Lundbeck Foundation (to P.G. through R133-A12689 and R313-2019-774); The Independent Research Fund Denmark (to P.G. through 4183-00559); NordForsk (to P.G. through 82000); UK Biotechnology \& Biosciences Research Council (to R.M.B. and P.K. through BB/P025927/1); P.K. is the recipient of an Aston University 50th Anniversary Prize Fellowship: M.M.S. is supported through funding through funding by Leverhulme Trust (ECF-2021-602 ). ",

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doi = "10.1016/j.xpro.2022.101316",

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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

N1 - © 2022 The Authors. This is an open access article under the CC BY license 4.0 Funding Information: We acknowledge the Swedish Research Council (to S.T.-H. through 2013-05945 and 2019-06106); the Crafoord Foundation (to S.T.-H. through 20140811 and 20180916); the Magnus Bergvall Foundation (to S.T.-H. through 2015-01534); the Knut and Alice Wallenberg Foundation (to P.G. through KAW 2015.0131 and 2020.0194); the Lundbeck Foundation (to P.G. through R133-A12689 and R313-2019-774); The Independent Research Fund Denmark (to P.G. through 4183-00559); NordForsk (to P.G. through 82000); UK Biotechnology & Biosciences Research Council (to R.M.B. and P.K. through BB/P025927/1); P.K. is the recipient of an Aston University 50th Anniversary Prize Fellowship: M.M.S. is supported through funding through funding by Leverhulme Trust (ECF-2021-602 ).

PY - 2022/6/17

Y1 - 2022/6/17

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 - Humans

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KW - Homeostasis

KW - Single-molecule Assays

KW - Proteins - metabolism

KW - Aquaporins - metabolism

KW - Protein Biochemistry

KW - Proteins/metabolism

KW - Aquaporins/metabolism

UR - https://www.sciencedirect.com/science/article/pii/S2666166722001964?via%3Dihub

UR - https://www.scopus.com/pages/publications/85128271354

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DO - 10.1016/j.xpro.2022.101316

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VL - 3

JO - STAR protocols

JF - STAR protocols

IS - 2

M1 - 101316

ER -

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

Abstract

Bibliographical note

Keywords

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