ArticleBiophysical journal1999
Rundown of the hyperpolarization-activated KAT1 channel involves slowing of the opening transitions regulated by phosphorylation.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 35 citations in OpenAlex.
- A charged existence: A century of transmembrane ion transport in plants.Plant physiology · 2024Review
- Fusicoccin Activates KAT1 Channels by Stabilizing Their Interaction with 14-3-3 Proteins.The Plant cell · 2017Article
- Three types of single voltage-dependent potassium channels in the sarcolemma of frog skeletal muscle.The Journal of membrane biology · 2009Article
- 30-year progress of membrane transport in plants.Planta · 2006Review
- A unique voltage sensor sensitizes the potassium channel AKT2 to phosphoregulation.The Journal of general physiology · 2005Article
- Physical and functional interaction of the Arabidopsis K(+) channel AKT2 and phosphatase AtPP2CA.The Plant cell · 2002Article
- Histidine(118) in the S2-S3 linker specifically controls activation of the KAT1 channel expressed in Xenopus oocytes.Biophysical journal · 2000Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Disappearance of the functional activity or rundown of ion channels upon patch excision in many cells involves a decrease in the number of channels available to open. A variety of cellular and biophysical mechanisms have been shown to be involved in the rundown of different ion channels. We examined the rundown process of the plant hyperpolarization-activated KAT1 K+ channel expressed in Xenopus oocytes. The decrease in the KAT1 channel activity on patch excision was accompanied by progressive slowing of the activation time course, and it was caused by a shift in the voltage dependence of the channel without any change in the single-channel amplitude. The single-channel analysis showed that patch excision alters only the transitions leading up to the burst states of the channel. Patch cramming or concurrent application of protein kinase A (PKA) and ATP restored the channel activity. In contrast, nonspecific alkaline phosphatase (ALP) accelerated the rundown time course. Low internal pH, which inhibits ALP activity, slowed the KAT1 rundown time course. The results show that the opening transitions of the KAT1 channel are enhanced not only by hyperpolarization but also by PKA-mediated phosphorylation.
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Registered trials
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