|
KMID : 0578320210440040214
|
|
Molecules and Cells
2021 Volume.44 No. 4 p.214 ~ p.222
|
|
|
The Peroxisomal Localization of Hsd17b4 Is Regulated by Its Interaction with Phosphatidylserine
|
|
Lee Sang-Ah
Lee Ju-Yeon
Kim Kwan-Hyeong
Moon Hyun-Ji
Min Chan-Hyuk
Moon Byeong-Jin
Kim Deok-Hwan
Yang Susumin
Park Hyun-Jin
Lee Gwang-Rog
Park Rae-Kil
Park Dae-Ho
|
|
|
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.
|
|
|
KEYWORD
|
|
|
efferocytosis, exposure, Hsd17b4, interaction, peroxisome, phosphatidylserine
|
|
|
FullTexts / Linksout information
|
|
|
|
|
|
Listed journal information
|
|
  
|
|