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Literature summary for 3.1.4.4 extracted from

  • Rudge, S.A.; Wakelam, M.J.
    Inter-regulatory dynamics of phospholipase D and the actin cytoskeleton (2009), Biochim. Biophys. Acta, 1791, 856-861.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
ARF GTPases all ARF proteins 1-6 stimulate PLD to a similar extent Mus musculus
ARF GTPases all ARF proteins 1-6 stimulate PLD to a similar extent Rattus norvegicus
ARF GTPases all ARF proteins 1-6 stimulate PLD1 and PLD2 to a similar extent Homo sapiens
Cdc42 in addition to interactions with Rac and Rho, PLD1 is regulated by Cdc42 Mus musculus
Cdc42 in addition to interactions with Rac and Rho, PLD1 is regulated by Cdc42 Homo sapiens
Cdc42 in addition to interactions with Rac and Rho, PLD1 is regulated by Cdc42 Rattus norvegicus
Rho GTPases PLD1 and PLD2 activity is regulated by the Rho family of small GTPases Mus musculus
Rho GTPases PLD1 and PLD2 activity is regulated by the Rho family of small GTPases Homo sapiens
Rho GTPases PLD1 and PLD2 activity is regulated by the Rho family of small GTPases Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information addition of PLD from Streptomyces chromofocus of exogenous PtdOH causes the normally semiround Hamster IIC9 fibroblasts to become more elongated in shape. Moreover, the PLD and PtdOH-induced change in cell morphology is driven by the formation of actin stress fibres Streptomyces chromofuscus

Localization

Localization Comment Organism GeneOntology No. Textmining
intracellular phosphorylation of cofilin on Ser3 by LIM-kinase 1 correlates with a relocalisation of PLD1 from a predominantly intracellular localisation to the plasma membrane Mus musculus 5622
-
intracellular phosphorylation of cofilin on Ser3 by LIM-kinase 1 correlates with a relocalisation of PLD1 from a predominantly intracellular localisation to the plasma membrane Homo sapiens 5622
-
intracellular phosphorylation of cofilin on Ser3 by LIM-kinase 1 correlates with a relocalisation of PLD1 from a predominantly intracellular localisation to the plasma membrane Rattus norvegicus 5622
-
plasma membrane phosphorylation of cofilin on Ser3 by LIM-kinase 1 correlates with a relocalisation of PLD1 from a predominantly intracellular localisation to the plasma membrane Mus musculus 5886
-
plasma membrane phosphorylation of cofilin on Ser3 by LIM-kinase 1 correlates with a relocalisation of PLD1 from a predominantly intracellular localisation to the plasma membrane Homo sapiens 5886
-
plasma membrane phosphorylation of cofilin on Ser3 by LIM-kinase 1 correlates with a relocalisation of PLD1 from a predominantly intracellular localisation to the plasma membrane Rattus norvegicus 5886
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
isozymes PLD1 and PLD2
-
Mus musculus
-
isozymes PLD1 and PLD2
-
Rattus norvegicus
-
isozymes PLD1 and PLD2
-
Streptomyces chromofuscus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
cell culture cells in suspension exhibit elevated levels of PLD activity compared to adherent cells, and as cells adhere to the substratum, PLD activity is downregulated Homo sapiens
-
endothelial cell
-
Homo sapiens
-
epithelial cell
-
Homo sapiens
-
fibroblast
-
Mus musculus
-
lymphocyte
-
Homo sapiens
-
mast cell
-
Homo sapiens
-
NIH-3T3 cell
-
Mus musculus
-
PC-12 cell
-
Rattus norvegicus
-
skin
-
Homo sapiens
-
stratum corneum
-
Homo sapiens
-

Synonyms

Synonyms Comment Organism
PLD
-
Streptomyces chromofuscus
PLD1
-
Mus musculus
PLD1
-
Homo sapiens
PLD1
-
Rattus norvegicus
PLD2
-
Mus musculus
PLD2
-
Homo sapiens
PLD2
-
Rattus norvegicus

General Information

General Information Comment Organism
metabolism the regulation of PLD activity by phosphoinositides, particularly by PtdIns(4,5)P2 provides a link with a number of proteins known to regulate cytoskeletal changes associated with adhesion and migration of cells, while this is also apparent when the additional PLD regulators, in particular the small GTPases, are considered Mus musculus
metabolism the regulation of PLD activity by phosphoinositides, particularly by PtdIns(4,5)P2 provides a link with a number of proteins known to regulate cytoskeletal changes associated with adhesion and migration of cells, while this is also apparent when the additional PLD regulators, in particular the small GTPases, are considered Homo sapiens
metabolism the regulation of PLD activity by phosphoinositides, particularly by PtdIns(4,5)P2 provides a link with a number of proteins known to regulate cytoskeletal changes associated with adhesion and migration of cells, while this is also apparent when the additional PLD regulators, in particular the small GTPases, are considered Rattus norvegicus
physiological function PLD is involved in stress fiber formation Streptomyces chromofuscus
physiological function PLD2 plays the role of master regulator and in an ill-defined manner regulates Rho function, PLD1 activity is downstream of this activation, however the generated phosphatidic acid controls changes in cytoskeletal organisation through its regulation of phosphatidylinositol-4-phosphate-5-kinase activity, overview. Regulatory mechanisms of PLD1 and PLD2 cellular activities, overview Mus musculus
physiological function PLD2 plays the role of master regulator and in an ill-defined manner regulates Rho function, PLD1 activity is downstream of this activation, however the generated phosphatidic acid controls changes in cytoskeletal organisation through its regulation of phosphatidylinositol-4-phosphate-5-kinase activity, overview. Regulatory mechanisms of PLD1 and PLD2 cellular activities, overview Rattus norvegicus
physiological function PLD2 plays the role of master regulator and in an ill-defined manner regulates Rho function, PLD1 activity is downstream of this activation, however the generated phosphatidic acid controls changes in cytoskeletal organisation through its regulation of phosphatidylinositol-4-phosphate-5-kinase activity, PLD2 master regulator model, overview. Relation between PLD activation and cytoskeletal remodelling, PLD signalling during cell adhesion, PLD regulation of integrin adhesiveness, cell spreading, and of actin polymerisation during cell spreading, regulation of of stress fibre formation, regulatory mechanisms of PLD1 and PLD2 cellular activities, overview. PLD signalling regulates actin-myosin contractility necessary for cell spreading Homo sapiens