Golgi membrane fission requires the CtBP1-S/BARS-induced activation of lysophosphatidic acid acyltransferase δ

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Pagliuso, Alessandro | Valente, Carmen | Giordano, Lucia Laura | Filograna, Angela | Li, Guiling | Circolo, Diego | Turacchio, Gabriele | Marzullo, Vincenzo Manuel | Mandrich, Luigi | Zhukovsky, Mikhail | Formiggini, Fabio | Polishchuk, Roman | Corda, Daniela | Luini, Alberto

Edité par CCSD ; Nature Publishing Group -

International audience. Membrane fission is an essential cellular process by which continuous membranes split into separate parts. We have previously identified CtBP1-S/BARS (BARS) as a key component of a protein complex that is required for fission of several endomembranes, including basolateral post-Golgi transport carriers. Assembly of this complex occurs at the Golgi apparatus, where BARS binds to the phosphoinositide kinase PI4KIIIβ through a 14-3-3γ dimer, as well as to ARF and the PKD and PAK kinases. We now report that, when incorporated into this complex, BARS binds to and activates a trans-Golgi lysophosphatidic acid (LPA) acyltransferase type δ (LPAATδ) that converts LPA into phosphatidic acid (PA); and that this reaction is essential for fission of the carriers. LPA and PA have unique biophysical properties, and their interconversion might facilitate the fission process either directly or indirectly (via recruitment of proteins that bind to PA, including BARS itself).

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