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

• Published in: Nature communications Vol. 15; no. 1; pp. 759 - 10
• Main Authors: Zhang, Weiqi, Ding, Dian, Lu, Yishuo, Chen, Hongyi, Jiang, Peijun, Zuo, Peng, Wang, Guangxi, Luo, Juan, Yin, Yue, Luo, Jianyuan, Yin, Yuxin
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 26.01.2024; Nature Publishing Group; Nature Portfolio
• Subjects: 101/28; 13/1; 13/31; 14/19; 14/35; 631/45/612/1222; 631/535/1258/1259; 631/57/2283; 692/699; 82/80; 82/83; Anion exchanging; Binding sites; Conformation; Humanities and Social Sciences; Lipids; multidisciplinary; Osteoclastogenesis; Phosphatidylinositol 4,5-diphosphate; Regulation; Regulatory mechanisms (biology); Science; Science (multidisciplinary); Structure-function relationships; Substrates; Transmembrane domains

Anion exchanger 2 (AE2) is an electroneutral Na + -independent Cl - /HCO 3 - 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 d...