Evidence map›Paper›PMID 11572962›Full record

ReviewProceedings of the National Academy of Sciences of the United States of America2001

Controlling potassium channel activities: Interplay between the membrane and intracellular factors.

B A Yi, D L Minor, Y F Lin, Y N Jan, L Y Jan

Open access · greenAbstract readReview
In one paragraph

Review in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 81 citations in OpenAlex.

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  20. Crystallization and preliminary X-ray diffraction studies of the tetramerization domain derived from the human potassium channel Kv1.3.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

B A YiDepartment of Physiology and Biochemistry, Howard Hughes Medical Institute, University of California, San Francisco, CA 94143, USA.
D L Minor
Y F Lin
Y N Jan
L Y Jan
University of California, San Francisco · USPain and Rehabilitation Medicine · US

Funding

GENETIC STUDIES OF THE SYNAPSER01NS015963 · NINDS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI JAN, LILY Y · 1985 to 2000
$109k
NINDS NIH HHS R01NS15963
6 · The paper itself

Abstract

Neural signaling is based on the regulated timing and extent of channel opening; therefore, it is important to understand how ion channels open and close in response to neurotransmitters and intracellular messengers. Here, we examine this question for potassium channels, an extraordinarily diverse group of ion channels. Voltage-gated potassium (Kv) channels control action-potential waveforms and neuronal firing patterns by opening and closing in response to membrane-potential changes. These effects can be strongly modulated by cytoplasmic factors such as kinases, phosphatases, and small GTPases. A Kv alpha subunit contains six transmembrane segments, including an intrinsic voltage sensor. In contrast, inwardly rectifying potassium (Kir) channels have just two transmembrane segments in each of its four pore-lining alpha subunits. A variety of intracellular second messengers mediate transmitter and metabolic regulation of Kir channels. For example, Kir3 (GIRK) channels open on binding to the G protein betagamma subunits, thereby mediating slow inhibitory postsynaptic potentials in the brain. Our structure-based functional analysis on the cytoplasmic N-terminal tetramerization domain T1 of the voltage-gated channel, Kv1.2, uncovered a new function for this domain, modulation of voltage gating, and suggested a possible means of communication between second messenger pathways and Kv channels. A yeast screen for active Kir3.2 channels subjected to random mutagenesis has identified residues in the transmembrane segments that are crucial for controlling the opening of Kir3.2 channels. The identification of structural elements involved in potassium channel gating in these systems highlights principles that may be important in the regulation of other types of channels.

Indexed as

Amino Acid SequenceAnimalsCell MembraneIon Channel GatingMacromolecular SubstancesModels, MolecularMolecular Sequence DataPotassium ChannelsProtein ConformationSignal TransductionMacromolecular SubstancesPotassium Channels

Identifiers

PMID11572962
PMCPMC58676
OpenAlexW2126744615

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.