ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2002
Phosphorylation-dependent and phosphorylation-independent modes of modulation of shaker family voltage-gated potassium channels by SRC family protein tyrosine kinases.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 58 citations in OpenAlex.
- Article
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- The atypical cadherin flamingo determines the competence of neurons for activity-dependent fine-scale topography.Molecular brain · 2019Article
- Margatoxin-bound quantum dots as a novel inhibitor of the voltage-gated ion channel Kv1.3.Journal of neurochemistry · 2017Article
- Ubiquitin ligase Nedd4-2 modulates Kv1.3 current amplitude and ion channel protein targeting.Journal of neurophysiology · 2016Article
- Hemopressin, an inverse agonist of cannabinoid receptors, inhibits neuropathic pain in rats.Peptides · 2014Article
- Synaptotagmin I delays the fast inactivation of Kv1.4 channel through interaction with its N-terminus.Molecular brain · 2014Article
- T-cell receptor activation decreases excitability of cortical interneurons by inhibiting α7 nicotinic receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- Serotonin contracts the rat mesenteric artery by inhibiting 4-aminopyridine-sensitive Kv channels via the 5-HT2A receptor and Src tyrosine kinase.Experimental & molecular medicine · 2013Article
- Control of voltage-gated potassium channel Kv2.2 expression by pyruvate-isocitrate cycling regulates glucose-stimulated insulin secretion.The Journal of biological chemistry · 2013Article
- Multifaceted modulation of K+ channels by protein-tyrosine phosphatase ε tunes neuronal excitability.The Journal of biological chemistry · 2012Article
- Dynamic modulation of the kv2.1 channel by SRC-dependent tyrosine phosphorylation.Journal of proteome research · 2012Article
- Systemic administration of anti-NGF increases A-type potassium currents and decreases pancreatic nociceptor excitability in a rat model of chronic pancreatitis.American journal of physiology. Gastrointestinal and liver physiology · 2012Article
- Ion channels in volume regulation of clonal kidney cells.Cell proliferation · 2010Article
- Hydrogen peroxide affects contractile activity and anti-oxidant enzymes in rat uterus.British journal of pharmacology · 2009Article
- Regulation of wild-type and mutant KCNQ1/KCNE1 channels by tyrosine kinase.Pflugers Archiv : European journal of physiology · 2009Article
- Genetic screening in C. elegans identifies rho-GTPase activating protein 6 as novel HERG regulator.Journal of molecular and cellular cardiology · 2009Article
- Brain-derived neurotrophic factor modulation of Kv1.3 channel is disregulated by adaptor proteins Grb10 and nShc.BMC neuroscience · 2009Article
- Identification of a functional interaction between Kv4.3 channels and c-Src tyrosine kinase.Biochimica et biophysica acta · 2008Article
- Oxidoreductase regulation of Kv currents in rat ventricle.Journal of molecular and cellular cardiology · 2008Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Modulation of voltage-gated potassium (Kv) channels by protein phosphorylation plays an essential role in the regulation of the membrane properties of cells. Protein-protein binding domains, such as Src homology 3 (SH3) domains, direct ion channel modulation by coupling the channels with intracellular signaling enzymes. The conventional view is that protein kinase binding to ion channels leads to modulation by bringing the channel substrate into physical proximity to the enzyme, thereby fostering covalent modification of the channel. The SH3 domain binding-dependent functional suppression of Kv1.5 currents by Src family protein tyrosine kinases (PTKs) is considered a canonical example of this type of mechanism. In the present study we address whether the SH3-dependent binding of Src family PTKs to Shaker family Kvs mediates modulatory events that are independent of and/or dependent on Src-catalyzed tyrosine phosphorylation of the channel. We find that Src binding and tyrosine phosphorylation are each able to modulate Kv1 family macroscopic channel currents independently. SH3-dependent binding of Src leads to the suppression of both Kv1.5 and Kv1.4 (modified to contain proline-rich SH3 domain binding sites) macroscopic currents even in the absence of Src-catalyzed tyrosine phosphorylation, whereas binding-independent tyrosine phosphorylation by Src leads to the suppression of Kv1.5 macroscopic currents and the modulation of Kv1.4 inactivation kinetics.
Indexed as
Identifiers
12223544PMC6758110W2151554161What OpenQuestion holds
Registered trials
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.