FSP27 and PLIN1 interaction promotes the formation of large lipid droplets in human adipocytes.

Research output: Contribution to journalArticle


title = "FSP27 and PLIN1 interaction promotes the formation of large lipid droplets in human adipocytes.",
abstract = "Human adipocytes express high levels of two distinct lipid droplet proteins, fat specific protein 27 (FSP27; also called CIDEC), a member of the CIDE family, and perilipin1 (PLIN1), a member of the PAT family. Both proteins play a role in fat metabolism in adipocytes, but how they interact is not known. Our present study demonstrates that FSP27 and PLIN1 co-localize and interact in cultured human primary adipocytes. We also found that the C-terminal domain of FSP27, aa 120-220, interacts with PLIN1. Individual expression of exogenous FSP27 or PLIN1 increased triglyceride content and decreased glycerol release (a measure of lipolysis), but co-expression of both proteins did not further increase triglyceride content or decrease lipolysis in human adipocytes. However, the combination of PLIN1 and FSP27 increased the average size of lipid droplets or caused the formation of unilocular adipocytes. Our data suggest that FSP27 interacts with PLIN1 to regulate lipid droplet size in human adipocytes in a concerted manner.",
keywords = "Adipocytes: metabolism, Carrier Proteins: metabolism, Phosphoproteins: metabolism, Proteins: genetics, Proteins: metabolism, Triglycerides: metabolism",
author = "{Tan Grahn}, {Hooi Min} and Yan Zhang and Mi-Jeong Lee and Sommer, {Andreia Gianotti} and Gustavo Mostoslavsky and Fried, {Susan K} and Greenberg, {Andrew S} and Vishwajeet Puri",
year = "2013",
doi = "10.1016/j.bbrc.2013.01.113",
language = "English",
volume = "432",
pages = "296--301",
journal = "Biochemical and Biophysical Research Communications",
issn = "1090-2104",
publisher = "Elsevier",
number = "2",