ArticleBiophysical journal2004
Histidines are responsible for zinc potentiation of the current in KDC1 carrot channels.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- External Cd2+ and protons activate the hyperpolarization-gated K+ channel KAT1 at the voltage sensor.The Journal of general physiology · 2021Article
- Salt Tolerance in Crops: Not Only a Matter of Gene Regulation.Plant physiology · 2017Article
- The effect of Silicon on photosynthesis and expression of its relevant genes in rice (Oryza sativa L.) under high-zinc stress.PloS one · 2014Article
- Preferential KAT1-KAT2 heteromerization determines inward K+ current properties in Arabidopsis guard cells.The Journal of biological chemistry · 2010Article
- The role of the C-terminus for functional heteromerization of the plant channel KDC1.Biophysical journal · 2009Article
- Heteromerization of Arabidopsis Kv channel alpha-subunits: Data and prospects.Plant signaling & behavior · 2008Article
- The zinc binding site of the Shaker channel KDC1 from Daucus carota.Biophysical journal · 2008Article
- KDC1, a carrot Shaker-like potassium channel, reveals its role as a silent regulatory subunit when expressed in plant cells.Plant molecular biology · 2008Article
- Stoichiometry studies reveal functional properties of KDC1 in plant shaker potassium channels.Biophysical journal · 2006Article
- Properties of shaker-type potassium channels in higher plants.The Journal of membrane biology · 2006Review
- Potassium and carrot embryogenesis: are K+ channels necessary for development?Plant molecular biology · 2004Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Unlike all plant inward-rectifying potassium channels, the carrot channel KDC1 has two histidine pairs (H161,H162) in the S3-S4 and (H224,H225) in the S5-S6 linkers. When coinjected with KAT1 in Xenopus oocytes, KDC1 participates in the formation of heteromultimeric KDC1:KAT1 channels and the ionic current is potentiated by extracellular Zn2+. To investigate the potential interactions between KDC1 and zinc, a KDC1-KAT1 dimer was constructed. The dimeric and heteromeric channels displayed similar characteristics and the same sensitivity to zinc and other metals; this result suggests that zinc binding is mediated by residues in a single channel subunit. The KDC1:KAT1 currents were also potentiated by external Pb2+ and Cd2+ and inhibited by Ni2+. To investigate further the role of KDC1-histidines, these amino acids were mutated into alanines. The single mutations H225A, H161A, and H162A did not affect the response of the heteromeric channels to zinc. Conversely, the single mutant H224A and the double mutants (H224A,H225A) and (H161A,H162A) abolished zinc potentiation, but not that induced by Pb2+ or Cd2+. These results suggest that Zn2+ potentiation cannot be ascribed to simple electrostatic interactions between zinc and channel residues and that histidine 224 is crucial for zinc but not for lead potentiation of the current.
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