[KSCI] Korea Science Citation Index Service

http://dx.doi.org/10.14348/molcells.2021.2217

The Peroxisomal Localization of Hsd17b4 Is Regulated by Its Interaction with Phosphatidylserine

Lee, Sang-Ah (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))
Lee, Juyeon (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))
Kim, Kwanhyeong (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))
Moon, Hyunji (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))
Min, Chanhyuk (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))
Moon, Byeongjin (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))
Kim, Deokhwan (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))
Yang, Susumin (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))
Park, Hyunjin (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))
Lee, Gwangrog (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))
Park, Raekil (Department of Biomedical Science and Engineering, GIST)
Park, Daeho (School of Life Sciences, Gwangju Institute of Science and Technology (GIST))

Abstract

Phosphatidylserine (PS), a negatively charged phospholipid exclusively located in the inner leaflet of the plasma membrane, is involved in various cellular processes such as blood coagulation, myoblast fusion, mammalian fertilization, and clearance of apoptotic cells. Proteins that specifically interact with PS must be identified to comprehensively understand the cellular processes involving PS. However, only a limited number of proteins are known to associate with PS. To identify PS-associating proteins, we performed a pulldown assay using streptavidin-coated magnetic beads on which biotin-linked PS was immobilized. Using this approach, we identified Hsd17b4, a peroxisomal protein, as a PS-associating protein. Hsd17b4 strongly associated with PS, but not with phosphatidylcholine or sphingomyelin, and the Scp-2-like domain of Hsd17b4 was responsible for this association. The association was disrupted by PS in liposomes, but not by free PS or the components of PS. In addition, translocation of PS to the outer leaflet of the plasma membrane enriched Hsd17b4 in peroxisomes. Collectively, this study suggests an unexpected role of PS as a regulator of the subcellular localization of Hsd17b4.

Keywords

efferocytosis; exposure; Hsd17b4; interaction; peroxisome; phosphatidylserine;

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