Unknown

Dataset Information

0

Ca2+-regulated Ca2+ channels with an RCK gating ring control plant symbiotic associations.


ABSTRACT: A family of plant nuclear ion channels, including DMI1 (Does not Make Infections 1) and its homologs CASTOR and POLLUX, are required for the establishment of legume-microbe symbioses by generating nuclear and perinuclear Ca2+ spiking. Here we show that CASTOR from Lotus japonicus is a highly selective Ca2+ channel whose activation requires cytosolic/nucleosolic Ca2+, contrary to the previous suggestion of it being a K+ channel. Structurally, the cytosolic/nucleosolic ligand-binding soluble region of CASTOR contains two tandem RCK (Regulator of Conductance for K+) domains, and four subunits assemble into the gating ring architecture, similar to that of large conductance, Ca2+-gated K+ (BK) channels despite the lack of sequence similarity. Multiple ion binding sites are clustered at two locations within each subunit, and three of them are identified to be Ca2+ sites. Our in vitro and in vivo assays also demonstrate the importance of these gating-ring Ca2+ binding sites to the physiological function of CASTOR as well as DMI1.

SUBMITTER: Kim S 

PROVIDER: S-EPMC6697748 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Ca<sup>2+</sup>-regulated Ca<sup>2+</sup> channels with an RCK gating ring control plant symbiotic associations.

Kim Sunghoon S   Kim Sunghoon S   Zeng Weizhong W   Bernard Shane S   Liao Jun J   Venkateshwaran Muthusubramanian M   Ane Jean-Michel JM   Jiang Youxing Y  

Nature communications 20190816 1


A family of plant nuclear ion channels, including DMI1 (Does not Make Infections 1) and its homologs CASTOR and POLLUX, are required for the establishment of legume-microbe symbioses by generating nuclear and perinuclear Ca<sup>2+</sup> spiking. Here we show that CASTOR from Lotus japonicus is a highly selective Ca<sup>2+</sup> channel whose activation requires cytosolic/nucleosolic Ca<sup>2+</sup>, contrary to the previous suggestion of it being a K<sup>+</sup> channel. Structurally, the cytoso  ...[more]

Similar Datasets

| S-EPMC7736618 | biostudies-literature
| S-EPMC3518701 | biostudies-literature
| S-EPMC9861210 | biostudies-literature
| S-EPMC6486743 | biostudies-literature
| S-EPMC7360967 | biostudies-literature
| S-EPMC9454758 | biostudies-literature
| S-EPMC5379921 | biostudies-literature
| S-EPMC6904572 | biostudies-literature
| S-EPMC5643522 | biostudies-literature
| S-EPMC8048425 | biostudies-literature