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

Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation.

The Journal of biological chemistry - 1 Jan 1999

Hu C D, Kariya K, Okada T, Qi X, Song C, Kataoka T

Abstract excerpt

Rap1A is phosphorylated by cAMP-dependent protein kinase (PKA), and this phosphorylation has been shown to modulate its interaction with other proteins. However, it is not known whether Rap1A phosphorylation is involved in regulation of its cellular functions, including suppression of Ras-dependent Raf-1 activation. We have previously shown that this suppressive activity of Rap1A is attributable to its greatly...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to COS Cells
Share to GTP-Binding Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Phosphorylation

Share to Protein Binding

Share to Recombinant Proteins

Source

Identifiers

PMID: 9867809
DOI: 10.1074/jbc.274.1.48

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Effect of phosphorylation on activities of Rap1A to interact with Raf-1 and to suppress Ras-dependent Raf-1 activation.PMID 9867809Read ↗

Protein kinase A-dependent phosphorylation of Rap1 regulates its membrane localization and cell migration.Semantic proximity Read ↗

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

Phosphorylation of rap1GAP in vivo and by cAMP-dependent kinase and the cell cycle p34cdc2 kinase in vitro.Semantic proximity Read ↗

Regulation of protein kinase A activity by p90 ribosomal S6 kinase 1.Semantic proximity Read ↗

Identification of a novel domain of Ras and Rap1 that directs their differential subcellular localizations.Semantic proximity Read ↗

Phosphorylation of GTP dissociation inhibitor by PKA negatively regulates RhoA.Semantic proximity Read ↗

RA-GEF-1, a guanine nucleotide exchange factor for Rap1, is activated by translocation induced by association with Rap1*GTP and enhances Rap1-dependent B-Raf activation.Semantic proximity Read ↗

Rap2 as a slowly responding molecular switch in the Rap1 signaling cascade.Semantic proximity Read ↗

Cyclic AMP Blocks Cell Growth through Raf-1-Dependent and Raf-1-Independent MechanismsSemantic proximity Read ↗

Cross-talk between sirtuin and mammalian target of rapamycin complex 1 (mTORC1) signaling in the regulation of S6 kinase 1 (S6K1) phosphorylation.Semantic proximity Read ↗

The strength of interaction at the Raf cysteine-rich domain is a critical determinant of response of Raf to Ras family small GTPases.Semantic proximity Read ↗

Phosphorylation of the catalytic subunit of protein kinase A. Autophosphorylation versus phosphorylation by phosphoinositide-dependent kinase-1.Semantic proximity Read ↗

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