ArticleThe Biochemical journal2005
Amino acids in the pore region of Kv1 potassium channels dictate cell-surface protein levels: a possible trafficking code in the Kv1 subfamily.
Article in The Biochemical journal, 2005. 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, 26 citations in OpenAlex.
- Heterochannels Kv(1.1-1.2)Cells · 2025Article
- Potassium KCa3.1 channel overexpression deteriorates functionality and availability of channels at the outer cellular membrane.Scientific reports · 2025Article
- New High-Affinity Peptide Ligands for Kv1.2 Channel: Selective Blockers and Fluorescent Probes.Cells · 2024Article
- Interactions of the Kv1.1 Channel with Peptide Pore Blockers: A Fluorescent Analysis on Mammalian Cells.Membranes · 2023Article
- Peptide Inhibitors of Kv1.5: An Option for the Treatment of Atrial Fibrillation.Pharmaceuticals (Basel, Switzerland) · 2021Review
- A Novel Insecticidal Spider Peptide that Affects the Mammalian Voltage-Gated Ion Channel hKv1.5.Frontiers in pharmacology · 2020Article
- The Role of the Carboxyl Terminus Helix C-D Linker in Regulating KCNQ3 K+ Current Amplitudes by Controlling Channel Trafficking.PloS one · 2015Article
- RNA editing in the central cavity as a mechanism to regulate surface expression of the voltage-gated potassium channel Kv1.1.The Journal of biological chemistry · 2014Article
- Putative pore-loops of TMEM16/anoctamin channels affect channel density in cell membranes.The Journal of physiology · 2013Article
- Depolarization and decreased surface expression of K+ channels contribute to NSAID-inhibition of intestinal restitution.Biochemical pharmacology · 2007Article
- Regulation of Kv1 channel trafficking by the mamba snake neurotoxin dendrotoxin K.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2007Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Kv1.1 and Kv1.4 potassium channels have different pore region determinants that were found to affect their cell-surface levels positively and negatively [Zhu, Watanabe, Gomez and Thornhill (2001) J. Biol. Chem. 276, 39419-39427; Zhu, Watanabe, Gomez and Thornhill (2003) J. Biol. Chem. 278, 25558-25567; Zhu, Watanabe, Gomez and Thornhill (2003) Biochem. J. 375, 761-768]. In the present study, we focused on the deep pore region of Kv1 members to test whether a cell-surface trafficking code was dictated by two amino acids. Kv1 channels with a threonine/lysine amino acid pair in a non-contiguous pore region promoted high surface levels, whereas a serine/tyrosine amino acid pair inhibited high surface expression by inducing a high level of partial endoplasmic reticulum retention. Our work suggests that a possible positive trafficking amino acid pair coding here for the Kv1 subfamily is Thr/Lys>Thr/Val>Thr/Tyr>Thr/Arg approximately Thr/His>Ser/Val>Ser/Tyr>Ser/Lys. The Kv1 trafficking code was not transferable to a Kv2 family member and thus it appears that it only governs surface levels in the context of its Kv1 native pore loop region and/or its S5 and S6 regions. All members of a given Kv2, Kv3 or Kv4 potassium channel subfamily have identical amino acids at similar positions in their deep pore regions (Thr/Tyr or Thr/Val), which suggests that any difference in surface levels among members is not dictated by these amino acids. Thus a major determinant for cell-surface trafficking of Kv1 potassium channels is an amino acid pair in their deep pore regions, whereas the cell-surface levels of a given Kv2, Kv3 or Kv4 subfamily member are probably not affected by these amino acids.
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