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

Role of phosphatidic acid in the coupling of the ERK cascade.

The Journal of biological chemistry - 26 Dec 2008

Kraft Catherine A, Garrido José Luis, Fluharty Eric, Leiva-Vega Luis, Romero Guillermo

Abstract excerpt

The production of phosphatidic acid plays a crucial role in the activation of the ERK cascade. This role was linked to the binding of phosphatidate to a specific polybasic site within the kinase domain of Raf-1. Here we show that phosphatidate promotes ERK phosphorylation in intact cells but does not activate Raf in vitro. The kinase suppressor of Ras (KSR) contains a sequence homologous to the phosphatidate...

Read the complete abstract on PubMed

Topics

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

Share to Arginine
Share to Cell Membrane
Share to Extracellular Signal-Regulated MAP Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Insulin

Share to Phosphatidic Acids

Share to Phosphorylation

Share to Proto-Oncogene Proteins c-raf

Share to Spectrophotometry

Source

Open in PubMed Open full text

Identifiers

PMID: 18952605
DOI: 10.1074/jbc.M804633200
PMCID: PMC2606017

Genes

KSR1

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

Role of phosphatidic acid in the coupling of the ERK cascade.PMID 18952605Read ↗

Phosphatidylserine binding is essential for plasma membrane recruitment and signaling function of 3-phosphoinositide-dependent kinase-1.Semantic proximity Read ↗

Regulation of ERK2 activity by dynamic <i>S</i> -acylationSemantic proximity Read ↗

Distinct utilization of effectors and biological outcomes resulting from site-specific Ras activation: Ras functions in lipid rafts and Golgi complex are dispensable for proliferation and transformation.Semantic proximity Read ↗

Phosphatidylinositol 4,5-biphosphate (PIP2) modulates interaction of syntaxin-1A with sulfonylurea receptor 1 to regulate pancreatic β-cell ATP-sensitive potassium channels.Semantic proximity Read ↗

Regulation of NHE3 by lysophosphatidic acid is mediated by phosphorylation of NHE3 by RSK2.Semantic proximity Read ↗

Coupling of endothelin receptors to the ERK/MAP kinase pathway. Roles of palmitoylation and G(alpha)q.Semantic proximity Read ↗

Functional analysis of a phosphatidic acid binding domain in human Raf-1 kinase: mutations in the phosphatidate binding domain lead to tail and trunk abnormalities in developing zebrafish embryos.Semantic proximity Read ↗

Reversible intracellular translocation of KRas but not HRas in hippocampal neurons regulated by Ca2+/calmodulin.Semantic proximity Read ↗

Raf kinase inhibitory protein regulates Raf-1 but not B-Raf kinase activation.Semantic proximity Read ↗

PKCε controls the fusion of secretory vesicles in mast cells in a phosphatidic acid-dependent mode.Semantic proximity Read ↗

Depalmitoylated Ras traffics to and from the Golgi complex via a nonvesicular pathway.Semantic proximity Read ↗

Role of the CDC25 homology domain of phospholipase Cepsilon in amplification of Rap1-dependent signaling.Semantic proximity Read ↗

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