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J. Biol. Chem., Vol. 281, Issue 20, 14232-14240, May 19, 2006

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MLDP, a Novel PAT Family Protein Localized to Lipid Droplets and Enriched in the Heart, Is Regulated by Peroxisome Proliferator-activated Receptor ^*

Tomohiro Yamaguchi¹, Shuhei Matsushita¹, Kiyoto Motojima, Fumiko Hirose, and Takashi Osumi²

From the Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori, Hyogo, 678-1297, Japan and the Department of Biochemistry, Meiji Pharmaceutical University, Kiyose, Tokyo 204-8588, Japan

Cytosolic lipid droplets (LDs) are multifunctional organelles that exist in all types of eukaryotic cells and control lipid homeostasis. In mammalian cells LDs contain a class of proteins in their surface layers that share a homologous sequence called the PAT domain, including perilipin, adipose differentiation-related protein (ADRP), a tail-interacting protein of 47 kDa (TIP47), and S3-12, which are distributed tissue- or cell type-selectively. Expression in some cases is regulated by peroxisome proliferator-activated receptors (PPARs). In this study we identified a new PAT family member named MLDP (myocardial LD protein) in a murine cDNA data base and showed the mRNA and protein to be highly enriched in the heart and also expressed at lower levels in the liver and adrenals. Upon subcellular fractionation, a substantial amount of MLDP was detected in the top fraction enriched with LDs. Furthermore, overexpressed MLDP tagged with green fluorescent protein accumulated at the surfaces of LDs and co-localized with perilipin and ADRP. Deletion analysis demonstrated the N-terminal region containing a PAT-1 domain and the following 33-mer domain to be required for targeting of MLDP to LDs. MLDP was found to be up-regulated at both mRNA and protein levels in the heart and liver by a selective ligand for PPAR, Wy14,643, but not in PPAR knock-out mice. MLDP expression was also increased upon fasting in parallel with ADRP. These results indicate that MLDP is a bona fide new PAT family member localized in LDs. Its expression depends on the physiological conditions and the action of PPAR.

Received for publication, February 22, 2006 , and in revised form, March 27, 2006.

^* This work was supported in part by grants from the ONO Medical Research Foundation and Hyogo Science and Technology Association (to T. Y.), grants-in-aid for Scientific Research from the Japan Society for the Promotion of Science, and by a 21st Century Center of Excellence (COE) Program. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ Both authors contributed equally to this work.

² To whom correspondence should be addressed. Tel.: 81-791-58-0194; Fax: 81-791-58-0193; E-mail: osumi{at}sci.u-hyogo.ac.jp.

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