Elucidating the role of lipid interactions in stabilizing the membrane protein KcsA.

Pei Qiao, Melanie T Odenkirk, Weiyi Zheng, Yuchen Wang, Jinhui Chen, Wenhao Xu, Erin S Baker

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Article in Biophysical journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

7 authors.

Pei QiaoCollege of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China; Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas. Electronic address: peiq@zjut.edu.cn.

Melanie T OdenkirkDepartment of Chemistry, North Carolina State University, Raleigh, North Carolina.

Weiyi ZhengCollege of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China.

Yuchen WangCollege of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China.

Jinhui ChenCollege of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou, China.

Wenhao XuCollaborative Innovation Center of Yangtze River Delta Region Green Pharmaceuticals, Zhejiang University of Technology, Hangzhou, China.

Erin S BakerDepartment of Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina.

Funding

Understanding the role of lipids in structure and function of membrane proteinsRM1GM145416 · NIGMS · TEXAS A&M UNIVERSITY · PI Erin S Baker, Arthur D Laganowsky · 2022 to 2026

$7.4M

NIGMS NIH HHS RM1 GM145416

6 · The paper itself

Abstract

The significant effects of lipid binding on the functionality of potassium channel KcsA have been validated by brilliant studies. However, the specific interactions between lipids and KcsA, such as binding parameters for each binding event, have not been fully elucidated. In this study, we employed native mass spectrometry to investigate the binding of lipids to KcsA and their effects on the channel. The tetrameric structure of KcsA remains intact even in the absence of lipid binding. However, the subunit architecture of the E71A mutant, which is constantly open at low pH, relies on tightly associated copurified lipids. Furthermore, we observed that lipids exhibit weak binding to KcsA at high pH when the channel is at a closed/inactivation state in the absence of permeant cation K

Indexed as

Bacterial ProteinsPotassium ChannelsProtein BindingStreptomyces lividansEscherichia coliHydrogen-Ion ConcentrationProtein StabilityBacterial ProteinsPotassium Channelsprokaryotic potassium channel

Identifiers

PMID39030907

DOI10.1016/j.bpj.2024.07.019

PMCPMC11427772

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.