Any feedback?
Literature summary for 3.1.4.4 extracted from
- The roles of phospholipase D in EGFR signaling (2009), Biochim. Biophys. Acta, 1791, 862-868.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| Arf1 protein | activates PLD2 and PLD1 in vitro | Cricetulus griseus | |
| Arf1 protein | activates PLD2 and PLD1 in vitro | Mus musculus | |
| Arf1 protein | activates PLD2 and PLD1 in vitro | Homo sapiens | |
| Arf1 protein | activates PLD2 and PLD1 in vitro | Rattus norvegicus | |
| Arf1 protein | activates PLD2 and PLD1 in vitro | Bos taurus | |
| Arf1 protein | activates PLD2 and PLD1 in vitro | Oryctolagus cuniculus | |
| Arf4 protein | in 293T cells overexpressing EGFR, Arf4 associates with the cytoplasmic region of EGFR and directly regulates PLD2 activation, but not PLD1 activation | Homo sapiens | |
| dynamin | a large GTPase, can interact with PLD in a GTP dependent manner in vitro | Cricetulus griseus | |
| dynamin | a large GTPase, can interact with PLD in a GTP dependent manner in vitro | Mus musculus | |
| dynamin | a large GTPase, can interact with PLD in a GTP dependent manner in vitro | Homo sapiens | |
| dynamin | a large GTPase, can interact with PLD in a GTP dependent manner in vitro | Rattus norvegicus | |
| dynamin | a large GTPase, can interact with PLD in a GTP dependent manner in vitro | Bos taurus | |
| dynamin | a large GTPase, can interact with PLD in a GTP dependent manner in vitro | Oryctolagus cuniculus | |
| additional information | epidermal growth factor triggers the activation of PLD in various cell types, such as a bovine luteal cell line | Bos taurus | |
| additional information | epidermal growth factor triggers the activation of PLD in various cell types, such as a Chinese hamster lung fibroblast cell line, CCL39, and a Chinese hamster embryo fibroblast cell line, IIC9 | Cricetulus griseus | |
| additional information | epidermal growth factor triggers the activation of PLD in various cell types, such as calvarial osteoblastic cells and 3Y1 rat fibroblasts | Rattus norvegicus | |
| additional information | epidermal growth factor triggers the activation of PLD in various cell types, such as immortalized rabbit corneal epithelial cells | Oryctolagus cuniculus | |
| additional information | epidermal growth factor triggers the activation of PLD in various cell types, such as mouse embryo fibroblasts, MEFs, a mouse myoblast cell line, C2C12, and a mouse embryo fibroblast cell line Swiss 3T3 | Mus musculus | |
| additional information | epidermal growth factor triggers the activation of PLD in various cell types, such as osteoblastic cells, a human embryonic kidney cell line HEK-293, a human epidermoid carcinoma cell line A-431, a human cervical cancer cell line HeLa, and human dermal fibroblasts | Homo sapiens | |
| Rac1 | PLD activation by EGF is dependent on Rac1, and not on PKC, in Rat1 fibroblasts | Rattus norvegicus | |
| RhoA | mediates PDGF-induced PLD activation in Rat1 fibroblasts | Rattus norvegicus |  |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | dominant negative Rac1, N17Rac1, completely inhibits PLD activation by EGF, but not by PDGF. Dominant-negative RalA and Ras also abolish PLD activation by EGF | Rattus norvegicus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| phosphatidylcholine + H2O | Cricetulus griseus | - |
choline + phosphatidic acid | - |
? | |
| phosphatidylcholine + H2O | Mus musculus | - |
choline + phosphatidic acid | - |
? | |
| phosphatidylcholine + H2O | Homo sapiens | - |
choline + phosphatidic acid | - |
? | |
| phosphatidylcholine + H2O | Rattus norvegicus | - |
choline + phosphatidic acid | - |
? | |
| phosphatidylcholine + H2O | Bos taurus | - |
choline + phosphatidic acid | - |
? | |
| phosphatidylcholine + H2O | Oryctolagus cuniculus | - |
choline + phosphatidic acid | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bos taurus | - |
isozymes PLD1 and PLD2 | - |
| Cricetulus griseus | - |
- |
- |
| Homo sapiens | - |
isozymes PLD1 and PLD2 | - |
| Mus musculus | - |
isozymes PLD1 and PLD2 | - |
| Oryctolagus cuniculus | - |
isozymes PLD2 and PLD1 | - |
| Rattus norvegicus | - |
isozymes PLD1 and PLD2 | - |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| 3Y1-B clone 1 cell | fibroblast cell line | Rattus norvegicus | - |
| A-431 cell | - |
Homo sapiens | - |
| C2C12 cell | - |
Mus musculus | - |
| DEDE cell | - |
Cricetulus griseus | - |
| epithelial cell | corneal | Oryctolagus cuniculus | - |
| fibroblast | - |
Rattus norvegicus | - |
| fibroblast | dermal | Homo sapiens | - |
| HEK-293 cell | - |
Homo sapiens | - |
| HeLa cell | - |
Homo sapiens | - |
| IIC9 cell | - |
Cricetulus griseus | - |
| lutein cell | - |
Bos taurus | - |
| NIH-3T3 cell | - |
Mus musculus | - |
| osteoblast | - |
Homo sapiens | - |
| osteoblast | calvarial osteoblastic cell | Rattus norvegicus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| phosphatidylcholine + H2O | - |
Cricetulus griseus | choline + phosphatidic acid | - |
? | |
| phosphatidylcholine + H2O | - |
Mus musculus | choline + phosphatidic acid | - |
? | |
| phosphatidylcholine + H2O | - |
Homo sapiens | choline + phosphatidic acid | - |
? | |
| phosphatidylcholine + H2O | - |
Rattus norvegicus | choline + phosphatidic acid | - |
? | |
| phosphatidylcholine + H2O | - |
Bos taurus | choline + phosphatidic acid | - |
? | |
| phosphatidylcholine + H2O | - |
Oryctolagus cuniculus | choline + phosphatidic acid | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| PLD | - |
Cricetulus griseus |
| PLD | - |
Mus musculus |
| PLD | - |
Homo sapiens |
| PLD | - |
Rattus norvegicus |
| PLD | - |
Bos taurus |
| PLD | - |
Oryctolagus cuniculus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner | Cricetulus griseus |
| physiological function | roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner | Mus musculus |
| physiological function | roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner | Homo sapiens |
| physiological function | roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner | Rattus norvegicus |
| physiological function | roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner | Bos taurus |
| physiological function | roles of phospholipase D in epidermal growth factor receptor, EGFR, signaling, modelling, overview. Coordination of EGF signaling by the PX domain of PLD, detailed overview. PLD is a key mediator of EGFR function, and can be directly regulated by upstream binding partners in an EGF-dependent manner | Oryctolagus cuniculus |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
