Identification of lipid droplet structure-like/resident proteins in Caenorhabditis elegans

Subjects: Biology >> Biophysics >> Biochemistry & Molecular Biology submitted time 2016-05-12

Na, Huimin Zhang, Peng Chen, Yong Zhu, Xiaotong Liu, Yi Liu, Yangli Xie, Kang Yang, Fuquan Zhang, Hong Liu, Pingsheng Na, Huimin Zhang, Peng Zhu, Xiaotong Liu, Yangli Xie, Kang Xu, Ningyi Mak, Ho Yi Xu, Ningyi Mak, Ho Yi Yu, Yong

Abstract： The lipid droplet (LD) is a cellular organelle that stores neutral lipids in cells and has been linked with metabolic disorders. Caenorhabditis elegans has many characteristics which make it an excellent animal model for studying LDs. However, unlike in mammalian cells, no LD structure-like/resident proteins have been identified in C. elegans, which has limited the utility of this model for the study of lipid storage and metabolism. Herein based on three lines of evidence, we identified that MDT-28 and DHS-3 previously identified in C. elegans LD proteome were two LD structure-like/resident proteins. First, MDT-28 and DHS-3 were found to be the two most abundant LD proteins in the worm. Second, the proteins were specifically localized to LDs and we identified the domains responsible for this targeting in both proteins. Third and most importantly, the depletion of MDT-28 induced LD clustering while DHS-3 deletion reduced triacylglycerol content (TAG). We further characterized the proteins finding that MDT-28 was ubiquitously expressed in the intestine, muscle, hypodermis, and embryos, whereas DHS-3 was expressed mainly in intestinal cells. Together, these two LD structure-like/resident proteins provide a basis for future mechanistic studies into the dynamics and functions of LDs in C. elegans. (C) 2015 Elsevier B.V. All rights reserved.

Peer Review Status:Awaiting Review

 Hits 3236  Downloads 1586  Comment