scholarly journals Diversity of voltage-gated potassium channels and cyclic nucleotide-binding domain-containing channels in eukaryotes

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Ilya Pozdnyakov ◽  
Pavel Safonov ◽  
Sergei Skarlato

Abstract Voltage-gated potassium channels (Kv) and cyclic nucleotide-binding domain-containing cation channels HCN, CNG, and KCNH are the evolutionarily related families of ion channels in animals. Their homologues were found in several lineages of eukaryotes and prokaryotes; however, the actual phylogenetic and structural diversity of these ion channels remains unclear. In this work, we present a taxonomically broad investigation of evolutionary relationships and structural diversity of Kv, HCN, CNG, and KCNH and their homologues in eukaryotes focusing on channels from different protistan groups. We demonstrate that both groups of channels consist of a more significant number of lineages than it was shown before, and these lineages can be grouped in two clusters termed Kv-like channels and CNBD-channels. Moreover, we, for the first time, report the unusual two-repeat tandem Kv-like channels and CNBD-channels in several eukaryotic groups, i.e. dinoflagellates, oomycetes, and chlorarachniophytes. Our findings reveal still underappreciated phylogenetic and structural diversity of eukaryotic ion channel lineages.

Author(s):  
Christopher Pfleger ◽  
Jana Kusch ◽  
Mahesh Kondapuram ◽  
Tina Schwabe ◽  
Christian Sattler ◽  
...  

2008 ◽  
Vol 381 (3) ◽  
pp. 655-669 ◽  
Author(s):  
Stephen L. Altieri ◽  
Gina M. Clayton ◽  
William R. Silverman ◽  
Adrian O. Olivares ◽  
Enrique M. De La Cruz ◽  
...  

2017 ◽  
Vol 112 (3) ◽  
pp. 335a-336a
Author(s):  
Reinhard Seifert ◽  
Florian Windler ◽  
Wolfgang Bönigk ◽  
Heinz-Gerd Körschen ◽  
U. Benjamin Kaupp

FEBS Letters ◽  
2017 ◽  
Vol 591 (18) ◽  
pp. 2869-2878 ◽  
Author(s):  
Francisco Romero ◽  
Carmen Santana‐Calvo ◽  
Yoloxochitl Sánchez‐Guevara ◽  
Takuya Nishigaki

2012 ◽  
Vol 102 (3) ◽  
pp. 330a
Author(s):  
Maria J. Marques Carvalho ◽  
Ricardo S. Vieira Pires ◽  
Guillaume Gabant ◽  
Martine Cadene ◽  
João H. Morais Cabral

2000 ◽  
Vol 28 (4) ◽  
pp. 471-475 ◽  
Author(s):  
T. Arazi ◽  
B. Kaplan ◽  
R. Sunkar ◽  
H. Fromm

Recently we discovered a tobacco protein (designated NtCBP4) that modulates heavy-metal tolerance in transgenic plants. Structurally, NtCBP4 is similar to mammalian cyclic-nucleotide-gated non-selective cation channels containing six putative transmembrane domains, a predicted pore region, a conserved cyclic-nucleotide-binding domain, and a high-affinity calmodulin-binding site that coincides with its cyclic-nucleotide-binding domain. Transgenic tobacco expressing the plasma-membrane-localized NtCBP4 exhibit improved tolerance to Ni2+ and hypersensitivity to Pb2+, which are associated with a decreased accumulation of Ni2+ and an enhanced accumulation of Pb2+ respectively. Transgenic plants expressing a truncated version of NtCBP4, from which regulatory domains had been removed, have a different phenotype. Here we describe our approach to studying the involvement of NtCBP4 in heavy-metal tolerance and to elucidate its physiological role.


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