FIT2 organizes lipid droplet biogenesis with ER tubule-forming proteins and septins

Author:

Chen Fang12,Yan Bing1ORCID,Ren Jie12,Lyu Rui12,Wu Yanfang1,Guo Yuting1,Li Dong1ORCID,Zhang Hong12ORCID,Hu Junjie12ORCID

Affiliation:

1. National Laboratory of Biomacromolecules, Chinese Academy of Sciences Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China

2. University of Chinese Academy of Sciences, Beijing, China

Abstract

Lipid droplets (LDs) are critical for lipid storage and energy metabolism. LDs form in the endoplasmic reticulum (ER). However, the molecular basis for LD biogenesis remains elusive. Here, we show that fat storage–inducing transmembrane protein 2 (FIT2) interacts with ER tubule-forming proteins Rtn4 and REEP5. The association is mainly transmembrane domain based and stimulated by oleic acid. Depletion of ER tubule-forming proteins decreases the number and size of LDs in cells and Caenorhabditis elegans, mimicking loss of FIT2. Through cytosolic loops, FIT2 binds to cytoskeletal protein septin 7, an interaction that is also required for normal LD biogenesis. Depletion of ER tubule-forming proteins or septins delays nascent LD formation. In addition, FIT2-interacting proteins are up-regulated during adipocyte differentiation, and ER tubule-forming proteins, septin 7, and FIT2 are transiently enriched at LD formation sites. Thus, FIT2-mediated nascent LD biogenesis is facilitated by ER tubule-forming proteins and septins.

Funder

National Science Foundation of China

Strategic Priority Research Program

Chinese Academy of Sciences

National Key Research and Development Program

National Institutes of Health

Office of Research Infrastructure Programs

Publisher

Rockefeller University Press

Subject

Cell Biology

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