scholarly journals Structural rearrangements underlying ligand-gating in Kir channels

2012 ◽  
Vol 3 (1) ◽  
Author(s):  
Shizhen Wang ◽  
Sun-Joo Lee ◽  
Sarah Heyman ◽  
Decha Enkvetchakul ◽  
Colin G. Nichols
2021 ◽  
Author(s):  
Rodrigo S Reis ◽  
Jules Deforges ◽  
Romy R Schmidt ◽  
Jos H M Schippers ◽  
Yves Poirier

Abstract A large portion of eukaryotic genes are associated with noncoding, natural antisense transcripts (NATs). Despite sharing extensive sequence complementarity with their sense mRNAs, mRNA-NAT pairs elusively often evade dsRNA-cleavage and siRNA-triggered silencing. More surprisingly, some NATs enhance translation of their sense mRNAs by yet unknown mechanism(s). Here we show that translation enhancement of the rice (Oryza sativa) PHOSPHATE1.2 (PHO1.2) mRNA is enabled by specific structural rearrangements guided by its noncoding antisense RNA (cis-NATpho1.2). Their interaction in vitro revealed no evidence of widespread intermolecular dsRNA formation, but rather specific local changes in nucleotide base-pairing, leading to higher flexibility of PHO1.2 mRNA at a key high GC regulatory region inhibiting translation, approximately 350 nucleotides downstream of the start codon. Sense-antisense RNA interaction increased formation of the 80S complex in PHO1.2, possibly by inducing structural rearrangement within this inhibitory region, thus making this mRNA more accessible to 60S. This work presents a framework for nucleotide-resolution studies of functional mRNA-antisense pairs. One-sentence summary: Interaction between PHO1.2 mRNA and its cis-natural antisense transcript enhances translation via a mechanism involving a local conformational shift and disruption of a key inhibitory region.


Author(s):  
Iris G. Insogna ◽  
A. Lanes ◽  
L. Dobson ◽  
E. S. Ginsburg ◽  
C. Racowsky ◽  
...  

RSC Advances ◽  
2021 ◽  
Vol 11 (13) ◽  
pp. 7450-7453
Author(s):  
Xinyu Hu ◽  
Haishen Yang

A reversible pseudo-single-ligand-gated ion transportation switch of ON–OFF–ON type through pillar[6]arene and photoresponsive azobenzene as dual-role ligand.


2021 ◽  
Author(s):  
Gilad Gabay ◽  
Junli Zhang ◽  
German Federico Burguener ◽  
Tyson Howell ◽  
Hanchao Wang ◽  
...  

2021 ◽  
Vol 22 (5) ◽  
pp. 2520
Author(s):  
Alba Bellot-Saez ◽  
Rebecca Stevenson ◽  
Orsolya Kékesi ◽  
Evgeniia Samokhina ◽  
Yuval Ben-Abu ◽  
...  

Potassium homeostasis is fundamental for brain function. Therefore, effective removal of excessive K+ from the synaptic cleft during neuronal activity is paramount. Astrocytes play a key role in K+ clearance from the extracellular milieu using various mechanisms, including uptake via Kir channels and the Na+-K+ ATPase, and spatial buffering through the astrocytic gap-junction coupled network. Recently we showed that alterations in the concentrations of extracellular potassium ([K+]o) or impairments of the astrocytic clearance mechanism affect the resonance and oscillatory behavior of both the individual and networks of neurons. These results indicate that astrocytes have the potential to modulate neuronal network activity, however, the cellular effectors that may affect the astrocytic K+ clearance process are still unknown. In this study, we have investigated the impact of neuromodulators, which are known to mediate changes in network oscillatory behavior, on the astrocytic clearance process. Our results suggest that while some neuromodulators (5-HT; NA) might affect astrocytic spatial buffering via gap-junctions, others (DA; Histamine) primarily affect the uptake mechanism via Kir channels. These results suggest that neuromodulators can affect network oscillatory activity through parallel activation of both neurons and astrocytes, establishing a synergistic mechanism to maximize the synchronous network activity.


1988 ◽  
Vol 36 (2) ◽  
pp. 183-190 ◽  
Author(s):  
Mef Nilbert ◽  
Sverre Heim ◽  
Nils Mandahl ◽  
Ulla-Maria Flodérus ◽  
Helena Willén ◽  
...  

2003 ◽  
Vol 284 (4) ◽  
pp. C910-C917 ◽  
Author(s):  
Angelos-Aristeidis Konstas ◽  
Christoph Korbmacher ◽  
Stephen J. Tucker

Heteromultimerization between different inwardly rectifying (Kir) potassium channel subunits is an important mechanism for the generation of functional diversity. However, little is known about the mechanisms that control this process and that prevent promiscuous interactions in cells that express many different Kir subunits. In this study, we have examined the heteromeric assembly of Kir5.1 with other Kir subunits and have shown that this subunit exhibits a highly selective interaction with members of the Kir4.0 subfamily and does not physically associate with other Kir subunits such as Kir1.1, Kir2.1, and Kir6.2. Furthermore, we have identified regions within the Kir4.1 subunit that appear to govern the specificity of this interaction. These results help us to understand the mechanisms that control Kir subunit recognition and assembly and how cells can express many different Kir channels while maintaining distinct subpopulations of homo- and heteromeric channels within the cell.


2011 ◽  
Vol 47 (38) ◽  
pp. 10716 ◽  
Author(s):  
Bingsen Zhang ◽  
Xiaojuan Ni ◽  
Wei Zhang ◽  
Lidong Shao ◽  
Qiang Zhang ◽  
...  

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