The Peroxisomal Localization of Hsd17b4 Is Regulated by Its Interaction with Phosphatidylserine
| Autor: | Raekil Park, Hyunjin Park, Chanhyuk Min, Daeho Park, Byeongjin Moon, Susumin Yang, Sang-Ah Lee, Hyunji Moon, Kwanhyeong Kim, Juyeon Lee, Gwangrog Lee, Deokhwan Kim |
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| Rok vydání: | 2021 |
| Předmět: |
Hsd17b4
phosphatidylserine Phospholipid interaction Phosphatidylserines Mice 03 medical and health sciences chemistry.chemical_compound Myoblast fusion 0302 clinical medicine Phosphatidylcholine Peroxisomes Animals Humans peroxisome Peroxisomal Multifunctional Protein-2 Molecular Biology 030304 developmental biology efferocytosis 0303 health sciences Liposome Cell Biology General Medicine Phosphatidylserine Peroxisome Subcellular localization Cell biology Mice Inbred C57BL HEK293 Cells chemistry exposure Sphingomyelin 030217 neurology & neurosurgery Research Article |
| Zdroj: | Molecules and Cells |
| ISSN: | 0219-1032 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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