Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The protein-tyrosine phosphatase PTPMEG interacts with glutamate receptor delta 2 and epsilon subunits.

The Journal of biological chemistry - 26 May 2000

Hironaka K, Umemori H, Tezuka T, Mishina M, Yamamoto T

Abstract excerpt

Glutamate receptor (GluR) delta2 is selectively expressed in cerebellar Purkinje cells and plays a crucial role in cerebellum-dependent motor learning. Although GluRdelta2 belongs to an ionotropic GluR family, little is known about its pharmacological features and downstream signaling cascade. To study molecular mechanisms underlying GluRdelta2-dependent motor learning, we employed yeast two-hybrid screening to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Immunoblotting
Share to In Situ Hybridization
Share to Phosphotyrosine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Tyrosine Phosphatases

Share to Proto-Oncogene Proteins c-fyn

Share to Receptors, Glutamate

Share to Receptors, N-Methyl-D-Aspartate

Share to Yeasts

Source

Identifiers

PMID: 10748123
DOI: 10.1074/jbc.M909302199

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The protein-tyrosine phosphatase PTPMEG interacts with glutamate receptor delta 2 and epsilon subunits.PMID 10748123Read ↗

Identification of a juxtamembrane segment of the glutamate receptor delta2 subunit required for the plasma membrane localization.Semantic proximity Read ↗

Role of the internal Shank-binding segment of glutamate receptor delta2 in synaptic localization and cerebellar functions.Semantic proximity Read ↗

Rescue of abnormal phenotypes in delta2 glutamate receptor-deficient mice by the extracellular N-terminal and intracellular C-terminal domains of the delta2 glutamate receptor.Semantic proximity Read ↗

Glutamate receptor δ2 associates with metabotropic glutamate receptor 1 (mGluR1), protein kinase Cγ, and canonical transient receptor potential 3 and regulates mGluR1-mediated synaptic transmission in cerebellar Purkinje neurons.Semantic proximity Read ↗

The extreme C-terminus of GluRdelta2 is essential for induction of long-term depression in cerebellar slices.Semantic proximity Read ↗

Ca2+ permeability of the channel pore is not essential for the delta2 glutamate receptor to regulate synaptic plasticity and motor coordination.Semantic proximity Read ↗

The N-terminal domain of GluD2 (GluRdelta2) recruits presynaptic terminals and regulates synaptogenesis in the cerebellum in vivo.Semantic proximity Read ↗

Rescue of abnormal phenotypes of the delta2 glutamate receptor-null mice by mutant delta2 transgenes.Semantic proximity Read ↗

Transgenic rescue for characterizing orphan receptors: a review of delta2 glutamate receptor.Semantic proximity Read ↗

A new motif necessary and sufficient for stable localization of the delta2 glutamate receptors at postsynaptic spines.Semantic proximity Read ↗

The glutamate receptor-interacting protein family of GluR2-binding proteins is required for long-term synaptic depression expression in cerebellar Purkinje cells.Semantic proximity Read ↗

Altered intracellular localization of the glutamate receptor channel delta 2 subunit in weaver and reeler Purkinje cells.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.