The ZAR1 resistosome is a calcium-permeable channel triggering plant immune signaling
Coordinated regulation of heterochromatin inheritance by Dpb3–Dpb4 complex
This study demonstrates that the two conserved small histone-fold subunits of the DNA polymerase epsilon complex, Dpb3 and Dpb4, form a heterodimer and play an important role in coordinating the inheritance of histone hypoacetylation and H3K9 methylation during replication, and proposes a mechanism for how two processes are coordinated during replication.
Structure and activity of SLAC1 channels for stomatal signaling in leaves
- Ya-nan Deng, Hamdy Kashtoh, Yu-hang Chen
- Environmental ScienceProceedings of the National Academy of Sciences
- 29 April 2021
These studies define multiple sites of regulatory phosphorylation in the context of an atomic structure of the SLAC1 channel, providing a mechanistic understanding of the fine-tuning of channel activity and thereby of stomatal apertures in response to the environment.
Structural basis for activity of TRIC counter-ion channels in calcium release
- Xiaohui Wang, M. Su, Yu-hang Chen
- BiologyProceedings of the National Academy of Sciences
- 15 February 2019
It is shown that Ca2+ binding to TRIC channels stabilizes a nonconductive conformation; however, Ca2-free TRIC, as is generated during calcium release, frees a gating residue on a voltage-sensing helix to move out of blockage in response to membrane depolarization, which can restore polarization for continued calcium release.
Structural basis for conductance through TRIC cation channels
Electrophysiology and mutagenesis studies show that prokaryotic TRICs have similar functional properties to those of mammalianTRICs and implicate the three-fold axis in the allosteric regulation of the channel.
Cryo-EM structure and electrophysiological characterization of ALMT from Glycine max reveal a previously uncharacterized class of anion channels
The study uncovers the molecular basis for a previously uncharacterized class of anion channels and provides insights into the gating and modulation of the ALMT12/QUAC1 anion channel.
Ccp1 Homodimer Mediates Chromatin Integrity by Antagonizing CENP-A Loading.
Molecular basis for the R-type anion channel QUAC1 activity in guard cells
The structural and functional analyses reveal that QUAC1 functions as an inward rectifying anion channel and suggests a mechanism for malate-mediated channel activation, which uncovers the molecular basis for a novel class of anion channels and provides insights into the gating and modulation of the R-type anionChannel.