ATP-dependent modulation of MgtE in Mg2+ homeostasis

Atsuhiro Tomita, Mingfeng Zhang, Fei Jin, Wenhui Zhuang, Hironori Takeda, Tatsuro Maruyama, Masanori Osawa, Ken-ichi Hashimoto, Hisashi Kawasaki, Koichi Ito, Naoshi Dohmae, Ryuichiro Ishitani, Ichio Shimada, Zhiqiang Yan (), Motoyuki Hattori () and Osamu Nureki ()
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Atsuhiro Tomita: The University of Tokyo
Mingfeng Zhang: Fudan University
Fei Jin: Fudan University
Wenhui Zhuang: Fudan University
Hironori Takeda: Kyoto Sangyo University, Kamigamo-motoyama
Tatsuro Maruyama: The University of Tokyo, Hongo
Masanori Osawa: The University of Tokyo, Hongo
Ken-ichi Hashimoto: Tokyo Denki University
Hisashi Kawasaki: Tokyo Denki University
Koichi Ito: The University of Tokyo
Naoshi Dohmae: RIKEN Center for Sustainable Resource Science
Ryuichiro Ishitani: The University of Tokyo
Ichio Shimada: The University of Tokyo, Hongo
Zhiqiang Yan: Fudan University
Motoyuki Hattori: Fudan University
Osamu Nureki: The University of Tokyo

Nature Communications, 2017, vol. 8, issue 1, 1-11

Abstract: Abstract Magnesium is an essential ion for numerous physiological processes. MgtE is a Mg2+ selective channel involved in the maintenance of intracellular Mg2+ homeostasis, whose gating is regulated by intracellular Mg2+ levels. Here, we report that ATP binds to MgtE, regulating its Mg2+-dependent gating. Crystal structures of MgtE–ATP complex show that ATP binds to the intracellular CBS domain of MgtE. Functional studies support that ATP binding to MgtE enhances the intracellular domain affinity for Mg2+ within physiological concentrations of this divalent cation, enabling MgtE to function as an in vivo Mg2+ sensor. ATP dissociation from MgtE upregulates Mg2+ influx at both high and low intracellular Mg2+ concentrations. Using site-directed mutagenesis and structure based-electrophysiological and biochemical analyses, we identify key residues and main structural changes involved in the process. This work provides the molecular basis of ATP-dependent modulation of MgtE in Mg2+ homeostasis.

Date: 2017
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DOI: 10.1038/s41467-017-00082-w

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