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

Alessandro Pagliuso(Institute of Protein Biochemistry), Carmen Valente(Institute of Protein Biochemistry), Lucia Laura Giordano(Institute of Protein Biochemistry), Angela Filograna(Institute of Protein Biochemistry), Guiling Li(Institute of Protein Biochemistry), Diego Circolo(Institute of Protein Biochemistry), Gabriele Turacchio(Institute of Protein Biochemistry), Vincenzo Manuel Marzullo(SDN Istituto di Ricerca Diagnostica e Nucleare), Luigi Mandrich(Institute of Protein Biochemistry), Mikhail A. Zhukovsky(Institute of Protein Biochemistry), Fabio Formiggini(Italian Institute of Technology), Roman Polishchuk(Telethon Institute Of Genetics And Medicine), Daniela Corda(Institute of Protein Biochemistry), Alberto Luini(SDN Istituto di Ricerca Diagnostica e Nucleare)
Nature Communications
July 12, 2016
10.1038/ncomms12148
Cited by 113Open Access
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Abstract

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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