Title : RalA and PLD1 promote lipid droplet growth in response to nutrient withdrawal.

Pub. Date : 2021 Jul 27

PMID : 34320341






5 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Mechanistically, RalA performs this function through phospholipase D1 (PLD1), an enzyme that converts phosphatidylcholine (PC) to phosphatidic acid (PA) and that is recruited to lysosomes during nutrient stress in a RalA-dependent fashion. Phosphatidic Acids phospholipase D1 Homo sapiens
2 Mechanistically, RalA performs this function through phospholipase D1 (PLD1), an enzyme that converts phosphatidylcholine (PC) to phosphatidic acid (PA) and that is recruited to lysosomes during nutrient stress in a RalA-dependent fashion. Phosphatidic Acids phospholipase D1 Homo sapiens
3 Mechanistically, RalA performs this function through phospholipase D1 (PLD1), an enzyme that converts phosphatidylcholine (PC) to phosphatidic acid (PA) and that is recruited to lysosomes during nutrient stress in a RalA-dependent fashion. Phosphatidic Acids phospholipase D1 Homo sapiens
4 Mechanistically, RalA performs this function through phospholipase D1 (PLD1), an enzyme that converts phosphatidylcholine (PC) to phosphatidic acid (PA) and that is recruited to lysosomes during nutrient stress in a RalA-dependent fashion. Phosphatidic Acids phospholipase D1 Homo sapiens
5 Our data support a model in which RalA recruits PLD1 to lysosomes during nutrient deprivation to promote the localized production of PA and the recruitment of perilipin 3 to expanding LDs. Phosphatidic Acids phospholipase D1 Homo sapiens