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Membrane fluidity is regulated by the C-elegans transmembrane protein FLD-1 and its human homologs TLCD1/2

Journal article
Authors Mario Ruiz
Rakesh Bodhicharla
Emma Svensk
Ranjan Devkota
Kiran Busayavalasa
Henrik Palmgren
Marcus Ståhlman
Jan Borén
Marc Pilon
Published in eLife
Volume 7
ISSN 2050-084X
Publication year 2018
Published at Wallenberg Laboratory
Department of Chemistry and Molecular Biology
Institute of Medicine, Department of Molecular and Clinical Medicine
Language en
Keywords fatty-acid-composition, molecular-dynamics simulations, total lipid, extraction, docosahexaenoic acid, biological-membranes, domain, stability, mboat family, bume method, temperature, phospholipids
Subject categories Biochemistry and Molecular Biology


Dietary fatty acids are the main building blocks for cell membranes in animals, and mechanisms must therefore exist that compensate for dietary variations. We isolated C. elegans mutants that improved tolerance to dietary saturated fat in a sensitized genetic background, including eight alleles of the novel gene fld-1 that encodes a homolog of the human TLCD1 and TLCD2 transmembrane proteins. FLD-1 is localized on plasma membranes and acts by limiting the levels of highly membrane-fluidizing long-chain polyunsaturated fatty acid-containing phospholipids. Human TLCD1/2 also regulate membrane fluidity by limiting the levels of polyunsaturated fatty acid-containing membrane phospholipids. FLD-1 and TLCD1/2 do not regulate the synthesis of long-chain polyunsaturated fatty acids but rather limit their incorporation into phospholipids. We conclude that inhibition of FLD-1 or TLCD1/2 prevents lipotoxicity by allowing increased levels of membrane phospholipids that contain fluidizing long-chain polyunsaturated fatty acids.

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