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

Regulation of proto-Dbl by intracellular membrane targeting and protein stability.

The Journal of biological chemistry - 31 May 2002

Vanni Cristina, Mancini Patrizia, Gao Yuan, Ottaviano Catherine, Guo Fukun, Salani Barbara, Torrisi Maria Rosaria, Zheng Yi, Eva Alessandra

Abstract excerpt

The pleckstrin homology (PH) domain of onco-Dbl, a guanine nucleotide exchange factor (GEF) for Cdc42 and RhoA GTPases, interacts with phosphoinositides (PIPs). This interaction modulates both the GEF activity and the targeting to the plasma membrane of onco-Dbl. Conversely, we have previously shown that in proto-Dbl an intramolecular interaction between the N-terminal domain and the PH domain imposes a negative...

Read the complete abstract on PubMed

Topics

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

Share to 3T3 Cells
Share to cdc42 GTP-Binding Protein

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclin D1

Share to Guanine Nucleotide Exchange Factors

Share to Guanosine Diphosphate

Share to Guanosine Triphosphate

Share to JNK Mitogen-Activated Protein Kinases

Share to rhoA GTP-Binding Protein

Source

Identifiers

PMID: 11907027
DOI: 10.1074/jbc.M111025200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Regulation of proto-Dbl by intracellular membrane targeting and protein stability.PMID 11907027Read ↗

Modulation of oncogenic DBL activity by phosphoinositol phosphate binding to pleckstrin homology domain.Semantic proximity Read ↗

Oligomerization of DH domain is essential for Dbl-induced transformation.Semantic proximity Read ↗

Role of the C-terminal SH3 domain and N-terminal tyrosine phosphorylation in regulation of Tim and related Dbl-family proteins.Semantic proximity Read ↗

Auto-inhibition of the Dbl family protein Tim by an N-terminal helical motif.Semantic proximity Read ↗

Regulation of proto-oncogenic dbl by chaperone-controlled, ubiquitin-mediated degradation.Semantic proximity Read ↗

Structural insights into the activation of the RhoA GTPase by the lymphoid blast crisis (Lbc) oncoprotein.Semantic proximity Read ↗

RAPSYN-Mediated Neddylation of BCR-ABL Alternatively Determines the Fate of Philadelphia Chromosome-positive LeukemiaSemantic proximity Read ↗

On the mechanism of autoinhibition of the RhoA-specific nucleotide exchange factor PDZRhoGEF.Semantic proximity Read ↗

The focal adhesion and nuclear targeting capacity of the LIM-containing lipoma-preferred partner (LPP) protein.Semantic proximity Read ↗

An Autoinhibitory Role for the Pleckstrin Homology Domain of Interleukin-2-Inducible Tyrosine Kinase and Its Interplay with Canonical Phospholipid Recognition.Semantic proximity Read ↗

Phosphatidylinositol (3,4,5)-trisphosphate specifically interacts with the phox homology domain of phospholipase D1 and stimulates its activity.Semantic proximity Read ↗

Hierarchy of membrane-targeting signals of phospholipase D1 involving lipid modification of a pleckstrin homology domain.Semantic proximity Read ↗

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