Evidence map›Paper›PMID 11149959›Full record

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

A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors.

M N Nitabach, D A Llamas, R C Araneda, J L Intile, I J Thompson, Y I Zhou, T C Holmes

Open access · greenAbstract read
In one paragraph

Article 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 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.3field-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

22 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Use-dependent activation of neuronal Kv1.2 channel complexes.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  6. CRYPTOCHROME-mediated phototransduction by modulation of the potassium ion channel β-subunit redox sensor.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Regulation of Na(v)1.2 channels by brain-derived neurotrophic factor, TrkB, and associated Fyn kinase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2007
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Alpha7 neuronal nicotinic acetylcholine receptors are negatively regulated by tyrosine phosphorylation and Src-family kinases.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005
    Article
  17. Association/dissociation of a channel-kinase complex underlies state-dependent modulation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2005
    Article
  18. Article
  19. Subunit-specific modulation of KCNQ potassium channels by Src tyrosine kinase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2003
    Article
  20. 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

7 authors at 2 institutions in 1 country.

M N NitabachDepartment of Biology, New York University, New York, NY 10003, USA.
D A Llamas
R C Araneda
J L Intile
I J Thompson
Y I Zhou
T C Holmes
Columbia University · USNew York University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is an open question how ion channel subunits that lack protein-protein binding motifs become targeted and covalently modified by cellular signaling enzymes. Here, we show that Src-family protein tyrosine kinases (PTKs) bind to heteromultimeric Shaker-family voltage-gated potassium (Kv) channels by interactions between the Src homology 3 (SH3) domain and the proline-rich SH3 domain ligand sequence in the Shaker-family subunit Kv1.5. Once bound to Kv1.5, Src-family PTKs phosphorylate adjacent subunits in the Kv channel heteromultimer that lack proline-rich SH3 domain ligand sequences. This SH3-dependent tyrosine phosphorylation contributes to significant suppression of voltage-evoked currents flowing through the heteromultimeric channel. These results demonstrate that Kv1.5 subunits function as SH3-dependent adaptor proteins that marshal Src-family kinases to heteromultimeric potassium channel signaling complexes, and thereby confer functional sensitivity upon coassembled channel subunits that are themselves not bound directly to Src-family kinases by allowing their phosphorylation. This is a mechanism for information transfer between subunits in heteromultimeric ion channels that is likely to underlie the generation of combinatorial signaling diversity in the control of cellular electrical excitability.

Indexed as

Potassium Channels, Voltage-GatedAction PotentialsAmino Acid SubstitutionAnimalsCell LineDimerizationDNA, ComplementaryGenes, srcHippocampusHumansIon Channel GatingIon TransportKidneyKv1.2 Potassium ChannelKv1.4 Potassium ChannelKv1.5 Potassium ChannelDNA, ComplementaryFYN protein, humanKCNA2 protein, humanKCNA4 protein, humanKCNA5 protein, humanKv1.2 Potassium ChannelKv1.4 Potassium ChannelKv1.5 Potassium ChannelMacromolecular SubstancesNerve Tissue ProteinsOncogene Protein pp60(v-src)PotassiumPotassium ChannelsPotassium Channels, Voltage-GatedProto-Oncogene ProteinsProto-Oncogene Proteins c-fynRecombinant Fusion ProteinsRNA, Messengersrc-Family Kinases

Identifiers

PMID11149959
PMCPMC14652
OpenAlexW2151750070

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.