Advances in Plasma Membrane Ion Channels of Plant Cells

doi:10.11983/CBB18022

Abstract

Abstract: Multiple ions, including cations and anions, are involved in growth, development, reproduction and stress responses as essential nutrients, osmotic components, cofactors of proteins and signaling molecules in plants. Ion channels localized in the plasma membrane and endomembrane of plant cells are essential tunnels and dynamic regulators of ion flux across biological membranes and are involved in the direct regulation of ion homeostasis in plant cells. A large number of ion channels have been identified in diverse plant species, especially in the model plant Arabidopsis, in recent years. Many ion channels are localized in the plasma membrane, and their protein structure, ion selectivity and permeability, gating patterns, activity-regulating mechanisms and the functional coordinating mechanisms between different ion channels have been analyzed. In this review, we summarize the research progress on the plasma membrane ion channels of plant cells and discuss the outstanding questions.

Key words: ions, ion flux across membrane, ion channels, plasma membrane, plant cells

Yanqiu Tan,Shujing Sun,Jingyun Dong,Wei Xu,Lingling Wang,Yongfei Wang. Advances in Plasma Membrane Ion Channels of Plant Cells[J]. Chinese Bulletin of Botany, 2019, 54(1): 102-118.

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URL: https://www.chinbullbotany.com/EN/10.11983/CBB18022

https://www.chinbullbotany.com/EN/Y2019/V54/I1/102

Figures/Tables 6

Figure 1 Topological structure of a representative subunit and tetramers of Shaker family from Arabidopsis (modified from Sharma et al., 2013) (A) Topological structure of a Shaker subunit; (B) Diverse tetramers of K+ channels composed of Shaker members, including inward and outward K+ channels. S1-S6: Transmembrane domains 1-6; N/C termini: The amino terminal and carboxyl terminal; P: Pore region; +: With positive charged voltage sensor domain; cNBD: Cyclic nucleotide binding domain.

Figure 2 Putative protein structure of an Arabidopsis GLR member (Lam et al., 1998; Price et al., 2012) S1-S4: Transmembrane domains 1-4; LBD: Ligand binding domain; N/C termini: The amino terminal and carboxyl terminal

Figure 3 Protein structure of Arabidopsis MCA1 and MCA2 (A) and a molecular mechanism of how MCA1/2 channels are activated by the tension of plasma membrane (B) (Kamano et al., 2015) S: The transmembrane domain; EF: EF-hand Ca2+ binding domain; N/C termini: The amino terminal and carboxyl terminal

Figure 4 The putative protein structure of an OSCA member from Arabidopsis (modified from Yuan et al., 2014)

Figure 5 The putative protein structure of an ALMT member from Arabidopsis (modified from Sharma et al., 2016)

Figure 6 The topological structures of a SLAC1 subunit (A) and the structure of a SLAC1 channel as a trimer (B) (Vahisalu et al., 2008; Chen et al., 2010)

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