ArticleThe EMBO journal1999
Receptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 93 citations in OpenAlex.
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- Input-specific bidirectional regulation of hippocampal CA3 pyramidal cell excitability.The Journal of physiology · 2025Article
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- Intracellular ZnThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2019Article
- Rare variants in Protein tyrosine phosphatase, receptor type A (PTPRA) in schizophrenia: Evidence from a family based study.Schizophrenia research · 2019Article
- Slc7a5 regulates Kv1.2 channels and modifies functional outcomes of epilepsy-linked channel mutations.Nature communications · 2018Article
- Tyrosine phosphorylation of Kv1.5 is upregulated in intrauterine growth retardation rats with exaggerated pulmonary hypertension.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2017Article
- Extracellular redox sensitivity of Kv1.2 potassium channels.Scientific reports · 2017Article
- Determinants of frequency-dependent regulation of Kv1.2-containing potassium channels.Channels (Austin, Tex.) · 2016Article
- Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoprotein-mediated mammary epithelial cell motility.The Journal of biological chemistry · 2013Article
- Activity-dependent downregulation of D-type K+ channel subunit Kv1.2 in rat hippocampal CA3 pyramidal neurons.The Journal of physiology · 2013Article
- 5-HT2 receptors-mediated modulation of voltage-gated K+ channels and neurophysiopathological correlates.Experimental brain research · 2013Review
- Protein tyrosine phosphatase α in the dorsomedial striatum promotes excessive ethanol-drinking behaviors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013Article
- Multifaceted modulation of K+ channels by protein-tyrosine phosphatase ε tunes neuronal excitability.The Journal of biological chemistry · 2012Article
- Receptor type protein tyrosine phosphatases (RPTPs) - roles in signal transduction and human disease.Journal of cell communication and signaling · 2012Article
- Cytoplasmic domains and voltage-dependent potassium channel gating.Frontiers in pharmacology · 2012Article
- Article
- Receptor-like protein-tyrosine phosphatase α enhances cell surface expression of neural adhesion molecule NB-3.The Journal of biological chemistry · 2011Article
- Contribution of Kv1.2 voltage-gated potassium channel to D2 autoreceptor regulation of axonal dopamine overflow.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The phosphorylation state of a given tyrosine residue is determined by both protein tyrosine kinase (PTK) and protein tyrosine phosphatase (PTP) activities. However, little is known about the functional interaction of these opposing activities at the level of an identified effector molecule. G protein-coupled receptors (GPCRs), including the m1 muscarinic acetylcholine receptor (mAChR), regulate a tyrosine kinase activity that phosphorylates and suppresses current generated by the Kv1.2 potassium channel. We examined the possibility that PTPs also participate in this signaling pathway since the tyrosine phosphatase inhibitor vanadate increases the extent of both Kv1.2 phosphorylation and suppression. We show that an endogenous transmembrane tyrosine phosphatase, receptor tyrosine phosphatase alpha (RPTPalpha), becomes tyrosine phosphorylated and co-immunoprecipitates with Kv1.2 in a manner dependent on m1 receptor activation. The N- and C-termini of Kv1.2 are shown to bind RPTPalpha in vitro. Overexpression of RPTPalpha in Xenopus oocytes increases resting Kv1.2 current. Biochemical and electrophysiological analysis reveals that recruiting RPTPalpha to Kv1.2 functionally reverses the tyrosine kinase-induced phosphorylation and suppression of Kv1.2 current in mammalian cells. Taken together, these results identify RPTPalpha as a new target of m1 mAChR signaling and reveal a novel regulatory mechanism whereby GPCR-mediated suppression of a potassium channel depends on the coordinate and parallel regulation of PTK and PTP activities.
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