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-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells.

The Journal of biological chemistry - 8 Mar 2002

Han Jung Min, Kim Jae Ho, Lee Byoung Dae, Lee Sang Do, Kim Yong, Jung Yon Woo, Lee Sukmook, Cho Wonhwa, Ohba Motoi, Kuroki Toshio, Suh Pann-Ghill, Ryu Sung Ho

Abstract excerpt

Many studies have shown that protein kinase C (PKC) is an important physiological regulator of phospholipase D (PLD). However, the role of PKC in agonist-induced PLD activation has been mainly investigated with a focus on the PLD1, which is one of the two PLD isoenzymes (PLD1 and PLD2) cloned to...

Read the complete abstract on PubMed

Topics

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

Share to Benzopyrans
Share to Bradykinin
Share to Maleimides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to PC12 Cells

Share to Peptide Mapping

Share to Phospholipase D

Share to Protein Kinase C-delta

Share to Tetradecanoylphorbol Acetate

Source

Identifiers

PMID: 11744693
DOI: 10.1074/jbc.M108343200

Genes

PLD2
PLD1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-11744693-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells.PMID 11744693Read ↗

Sequential protein kinase C (PKC)-dependent and PKC-independent protein kinase D catalytic activation via Gq-coupled receptors: differential regulation of activation loop Ser(744) and Ser(748) phosphorylation.Semantic proximity Read ↗

Involvement of phospholipase D2 in lysophosphatidate-induced transactivation of platelet-derived growth factor receptor-beta in human bronchial epithelial cells.Semantic proximity Read ↗

A role of p44/42 mitogen-activated protein kinases in formyl-peptide receptor-mediated phospholipase D activity and oxidant production.Semantic proximity Read ↗

Protein kinase C phosphorylates protein kinase D activation loop Ser744 and Ser748 and releases autoinhibition by the pleckstrin homology domain.Semantic proximity Read ↗

Mechanisms of regulation of phospholipase D1 by protein kinase Calpha.Semantic proximity Read ↗

Protein kinase D (PKD) activation in intact cells through a protein kinase C-dependent signal transduction pathway.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 ↗

Activation of protein kinase D3 by signaling through Rac and the alpha subunits of the heterotrimeric G proteins G12 and G13.Semantic proximity Read ↗

Functional implications of post-translational modifications of phospholipases D1 and D2.Semantic proximity Read ↗

Dynamic re-distribution of protein kinase D (PKD) as revealed by a GFP-PKD fusion protein: dissociation from PKD activation.Semantic proximity Read ↗

Mechanisms of regulation of phospholipase D1 and D2 by the heterotrimeric G proteins G13 and Gq.Semantic proximity Read ↗

Phospholipase D is involved in myogenic differentiation through remodeling of actin cytoskeleton.Semantic proximity Read ↗

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