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DFCP1 associates with lipid droplets
Author(s) -
Gao Guangang,
Sheng Yuanyuan,
Yang Hongyuan,
Chua Boon Tin,
Xu Li
Publication year - 2019
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1002/cbin.11199
Subject(s) - endoplasmic reticulum , golgi apparatus , organelle , microbiology and biotechnology , phosphatidylinositol , lipid droplet , subcellular localization , function (biology) , wortmannin , biology , biochemistry , chemistry , signal transduction , cytoplasm
Abstract Double FYVE‐containing protein 1 (DFCP1) is ubiquitously expressed, participates in intracellular membrane trafficking and labels omegasomes through specific interactions with phosphatidylinositol‐3‐phosphate (PI3P). Previous studies showed that subcellular DFCP1 proteins display multi‐organelle localization, including in the endoplasmic reticulum (ER), Golgi apparatus and mitochondria. However, its localization and function on lipid droplets (LDs) remain unclear. Here, we demonstrate that DFCP1 localizes to the LD upon oleic acid incubation. The ER‐targeted domain of DFCP1 is indispensable for its LD localization, which is further enhanced by double FYVE domains. Inhibition of PI3P binding at the FYVE domain through wortmannin treatment or double mutation at C654S and C770S have no effect on DFCP1's LD localization. These show that the mechanisms for DFCP1 targeting the omegasome and LDs are different. DFCP1 deficiency in MEF cells causes an increase in LD number and reduces LD size. Interestingly, DFCP1 interacts with GTP‐bound Rab18, an LD‐associated protein. Taken together, our work demonstrates the dynamic localization of DFCP1 is regulated by nutritional status in response to cellular metabolism.