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

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

Journal of cell science - 1 Oct 2005

Lee Jun Sung, Kim Jong Hyun, Jang Il Ho, Kim Hyeon Soo, Han Jung Min, Kazlauskas Andrius, Yagisawa Hitoshi, Suh Pann-Ghill, Ryu Sung Ho

Abstract excerpt

Phospholipase D (PLD), which catalyzes the hydrolysis of phosphatidylcholine to phosphatidic acid and choline, plays key roles in cellular signal transduction by mediating extracellular stimuli including hormones, growth factors, neurotransmitters, cytokines and extracellular matrix molecules. The molecular mechanisms by which domains regulate the activity of PLD--especially the phox homology (PX) domain--have...

Read the complete abstract on PubMed

Topics

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

Share to Enzyme Activation
Share to Extracellular Signal-Regulated MAP Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Phosphatidylinositol Phosphates

Share to Phospholipase D

Share to Platelet-Derived Growth Factor

Share to Protein Structure, Tertiary

Share to Recombinant Fusion Proteins

Share to Sequence Alignment

Source

Identifiers

PMID: 16179605
DOI: 10.1242/jcs.02564

Genes

PLD1
PLD2

Variants

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

Phosphatidylinositol (3,4,5)-trisphosphate specifically interacts with the phox homology domain of phospholipase D1 and stimulates its activity.PMID 16179605Read ↗

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

The direct interaction of phospholipase C-gamma 1 with phospholipase D2 is important for epidermal growth factor signaling.Semantic proximity Read ↗

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

Functional Regulation of Phospholipase D Expression in Cancer and InflammationSemantic proximity Read ↗

Influence of phosphatidylinositol 4,5-bisphosphate on human phospholipase D1 wild-type and deletion mutants: is there evidence for an interaction of phosphatidylinositol 4,5-bisphosphate with the putative pleckstrin homology domain?Semantic proximity Read ↗

Structural insights into the regulation of PDK1 by phosphoinositides and inositol phosphates.Semantic proximity Read ↗

Dual role for phosphoinositides in regulation of yeast and mammalian phospholipase D enzymes.Semantic proximity Read ↗

Redefining the specificity of phosphoinositide-binding by human PH domain-containing proteinsSemantic proximity Read ↗

Phosphatidic acid regulation of PIPKI is critical for actin cytoskeletal reorganization.Semantic proximity Read ↗

Molecular modeling studies of the Akt PH domain and its interaction with phosphoinositides.Semantic proximity Read ↗

A comprehensive model that explains the regulation of phospholipase D2 activity by phosphorylation-dephosphorylation.Semantic proximity Read ↗

Tyrosine phosphorylation of protein kinase D in the pleckstrin homology domain leads to activation.Semantic proximity Read ↗

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