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Literature summary for 3.1.4.4 extracted from

  • Hodges, R.R.; Guilbert, E.; Shatos, M.A.; Natarajan, V.; Dartt, D.A.
    Phospholipase D1, but not D2, regulates protein secretion via Rho/ROCK in a Ras/Raf-independent, MEK-dependent manner in rat lacrimal gland (2011), Invest. Ophthalmol. Vis. Sci., 52, 2199-2210.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.4

Activating Compound

Activating Compound Comment Organism Structure
Carbachol PLD1 is activated by cholinergic agonists. Atropine inhibits this PLD1 activation Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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-
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Source Tissue

Source Tissue Comment Organism Textmining
epithelial cell primary, PLD1 Rattus norvegicus
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lacrimal gland acini Rattus norvegicus
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Synonyms

Synonyms Comment Organism
phospholipase D1
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 Rattus norvegicus
PLD1
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 Rattus norvegicus

General Information

General Information Comment Organism
metabolism identification of a signaling pathway for PLD in the lacrimal gland with Rho and ROCK1 activating PLD1, but not PLD2, in response to cholinergic agonists causing their association with one another. Formation of this signaling complex results in the downstream activation of MEK and ERK, but the activation is independent of the signaling molecules Ras, Raf, Pyk2, and cSrc, which usually activate ERK. Activation of ERK then attenuates cholinergic agonist-stimulated protein secretion. The muscarinic activation of PLD1 attenuates protein secretion by activating ERK Rattus norvegicus