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

Phosphorylation of Rap1GAP, a striatally enriched protein, by protein kinase A controls Rap1 activity and dendritic spine morphology.

Proceedings of the National Academy of Sciences of the United States of America - 3 Mar 2009

McAvoy Thomas, Zhou Ming-ming, Greengard Paul, Nairn Angus C

Abstract excerpt

Protein kinase A (PKA)-dependent signaling cascades play an important role in mediating the effects of dopamine and other neurotransmitters in striatal medium spiny neurons. We have identified a prominent striatal PKA substrate as Rap1-GTPase activating protein (Rap1GAP), a negative regulator of...

Read the complete abstract on PubMed

Topics

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

Share to Calcium
Share to Cyclic AMP
Share to Cyclic AMP-Dependent Protein Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Dendritic Spines

Share to GTPase-Activating Proteins

Share to rap GTP-Binding Proteins

Share to Substrate Specificity

Share to Tissue Culture Techniques

Source

Open in PubMed Open full text

Identifiers

PMID: 19218462
DOI: 10.1073/pnas.0813263106
PMCID: PMC2651273

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-19218462-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphorylation of Rap1GAP, a striatally enriched protein, by protein kinase A controls Rap1 activity and dendritic spine morphology.PMID 19218462Read ↗

Rhes influences striatal cAMP/PKA-dependent signaling and synaptic plasticity in a gender-sensitive fashion.Semantic proximity Read ↗

LRRK2 regulates synaptic function through modulation of actin cytoskeletal dynamicsSemantic proximity Read ↗

Dopamine D2 receptor signaling modulates mutant ataxin-1 S776 phosphorylation and aggregation.Semantic proximity Read ↗

Selective expression of a dominant-negative type Iα PKA regulatory subunit in striatal medium spiny neurons impairs gene expression and leads to reduced feeding and locomotor activity.Semantic proximity Read ↗

RasGRP1 (CalDAG-GEF-II) Mediates L-DOPA-induced Dyskinesia in a Mouse Model of Parkinson DiseaseSemantic proximity Read ↗

Signal transduction in l-DOPA-induced dyskinesia: from receptor sensitization to abnormal gene expressionSemantic proximity Read ↗

Ras and Rap control AMPA receptor trafficking during synaptic plasticity.Semantic proximity Read ↗

Cross-talk between LRRK2 and PKA: implication for Parkinson's disease?Semantic proximity Read ↗

Regulation of cortical dendrite development by Rap1 signaling.Semantic proximity Read ↗

The Protein Biochemistry of the Postsynaptic Density in Glutamatergic Synapses Mediates Learning in Neural Networks.Semantic proximity Read ↗

PKA/AKAP1 and PP2A/Bβ2 regulate neuronal morphogenesis via Drp1 phosphorylation and mitochondrial bioenergetics.Semantic proximity Read ↗

Phosphorylation of CalDAG-GEFI by protein kinase A prevents Rap1b activation.Semantic proximity Read ↗

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