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Structural and functional insights into the lipid regulation of human anion exchanger 2

Zhang, Weiqi ; Ding, Dian ; Lu, Yishuo ; Chen, Hongyi ; Jiang, Peijun ; Zuo, Peng ; Wang, Guangxi ; Luo, Juan ; Yin, Yue ; Luo, Jianyuan ; Yin, Yuxin

Nature communications, 2024-01, Vol.15 (1), p.759-759, Article 759 [Periódico revisado por pares]

England: Nature Publishing Group

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Título:
Structural and functional insights into the lipid regulation of human anion exchanger 2
Autor: Zhang, Weiqi ; Ding, Dian ; Lu, Yishuo ; Chen, Hongyi ; Jiang, Peijun ; Zuo, Peng ; Wang, Guangxi ; Luo, Juan ; Yin, Yue ; Luo, Jianyuan ; Yin, Yuxin
Assuntos: Anion exchanging ; Anion Transport Proteins - metabolism ; Antiporters - genetics ; Binding sites ; Chloride-Bicarbonate Antiporters - genetics ; Conformation ; Humans ; Hydrogen-Ion Concentration ; Lipids ; Mutation ; Osteoclastogenesis ; Phosphatidylinositol 4,5-diphosphate ; Regulation ; Regulatory mechanisms (biology) ; SLC4A Proteins ; Structure-function relationships ; Substrates ; Transmembrane domains
É parte de: Nature communications, 2024-01, Vol.15 (1), p.759-759, Article 759
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: Anion exchanger 2 (AE2) is an electroneutral Na -independent Cl /HCO exchanger belongs to the SLC4 transporter family. The widely expressed AE2 participates in a variety of physiological processes, including transepithelial acid-base secretion and osteoclastogenesis. Both the transmembrane domains (TMDs) and the N-terminal cytoplasmic domain (NTD) are involved in regulation of AE2 activity. However, the regulatory mechanism remains unclear. Here, we report a 3.2 Å cryo-EM structure of the AE2 TMDs in complex with PIP and a 3.3 Å full-length mutant AE2 structure in the resting state without PIP . We demonstrate that PIP at the TMD dimer interface is involved in the substrate exchange process. Mutation in the PIP binding site leads to the displacement of TM7 and further stabilizes the interaction between the TMD and the NTD. Reduced substrate transport activity and conformation similar to AE2 in acidic pH indicating the central contribution of PIP to the function of AE2.
Editor: England: Nature Publishing Group
Idioma: Inglês

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Structural and functional insights into the lipid regulation of human anion exchanger 2

Zhang, Weiqi ; Ding, Dian ; Lu, Yishuo ; Chen, Hongyi ; Jiang, Peijun ; Zuo, Peng ; Wang, Guangxi ; Luo, Juan ; Yin, Yue ; Luo, Jianyuan ; Yin, Yuxin

England: Nature Publishing Group

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