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Topological characterization of the mitochondrial phospholipid scramblase 3
Author(s) -
LuévanoMartínez Luis Alberto,
Kowaltowski Alicia J.
Publication year - 2017
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12917
Subject(s) - phospholipid scramblase , cardiolipin , intermembrane space , mitophagy , microbiology and biotechnology , mitochondrial intermembrane space , inner membrane , transmembrane protein , transmembrane domain , mitochondrion , membrane topology , inner mitochondrial membrane , phospholipid , translocase of the outer membrane , chemistry , biology , topology (electrical circuits) , bacterial outer membrane , biochemistry , mitochondrial membrane transport protein , membrane , phosphatidylserine , apoptosis , receptor , autophagy , mathematics , escherichia coli , combinatorics , gene
Scramblases redistribute phospholipids in biological membranes. Phospholipid scramblase 3 (PLSCR3), which is located in mitochondria, has been reported to be involved in cardiolipin distribution from the inner to the outer membrane, thus regulating cellular processes such as apoptosis or mitophagy. However, the localization and topology of this protein has not been convincingly addressed to support a role in intermembrane phospholipid transfer. Here, we studied PLSCR3 topology within mitochondria. We show that PLSCR3 inserts in the inner membrane (IM) via its C‐terminal transmembrane helix, whereas its N‐terminal portion is oriented toward the intermembrane space where it is activated by calcium. Our results suggest that PLSCR3, via its C‐terminal transmembrane domain, participates in the bidirectional movement of phospholipids within the IM.