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

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FSP27 and PLIN1 interaction promotes the formation of large lipid droplets in human adipocytes. / Tan Grahn, Hooi Min; Zhang, Yan; Lee, Mi-Jeong; Sommer, Andreia Gianotti; Mostoslavsky, Gustavo; Fried, Susan K; Greenberg, Andrew S; Puri, Vishwajeet.

In: Biochemical and Biophysical Research Communications, Vol. 432, No. 2, 2013, p. 296-301.

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Tan Grahn, Hooi Min ; Zhang, Yan ; Lee, Mi-Jeong ; Sommer, Andreia Gianotti ; Mostoslavsky, Gustavo ; Fried, Susan K ; Greenberg, Andrew S ; Puri, Vishwajeet. / FSP27 and PLIN1 interaction promotes the formation of large lipid droplets in human adipocytes. In: Biochemical and Biophysical Research Communications. 2013 ; Vol. 432, No. 2. pp. 296-301.

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TY - JOUR

T1 - FSP27 and PLIN1 interaction promotes the formation of large lipid droplets in human adipocytes.

AU - Tan Grahn, Hooi Min

AU - Zhang, Yan

AU - Lee, Mi-Jeong

AU - Sommer, Andreia Gianotti

AU - Mostoslavsky, Gustavo

AU - Fried, Susan K

AU - Greenberg, Andrew S

AU - Puri, Vishwajeet

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

KW - Adipocytes: metabolism

KW - Carrier Proteins: metabolism

KW - Phosphoproteins: metabolism

KW - Proteins: genetics

KW - Proteins: metabolism

KW - Triglycerides: metabolism

U2 - 10.1016/j.bbrc.2013.01.113

DO - 10.1016/j.bbrc.2013.01.113

M3 - Article

VL - 432

SP - 296

EP - 301

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 1090-2104

IS - 2

ER -