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

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  • Alessandro Pagliuso

    (Institute of Protein Biochemistry, National Research Council
    Telethon Institute of Genetics and Medicine (TIGEM)
    Present address: Institut Pasteur, Unité des Interactions Bactéries-Cellules, Département de Biologie Cellulaire et Infection, 25-28, rue du Docteur-Roux, 75015 Paris, France)

  • Carmen Valente

    (Institute of Protein Biochemistry, National Research Council)

  • Lucia Laura Giordano

    (Institute of Protein Biochemistry, National Research Council)

  • Angela Filograna

    (Institute of Protein Biochemistry, National Research Council)

  • Guiling Li

    (Institute of Protein Biochemistry, National Research Council
    Present address: Institute of Genomic Medicine, Wenzhou Medical University, Wenzhou, Zhejiang 325000, China)

  • Diego Circolo

    (Institute of Protein Biochemistry, National Research Council)

  • Gabriele Turacchio

    (Institute of Protein Biochemistry, National Research Council)

  • Vincenzo Manuel Marzullo

    (IRCCS SDN Istituto di Ricerca Diagnostica e Nucleare)

  • Luigi Mandrich

    (Institute of Protein Biochemistry, National Research Council)

  • Mikhail A. Zhukovsky

    (Institute of Protein Biochemistry, National Research Council)

  • Fabio Formiggini

    (Italian Institute of Technology, Centre for Advanced Biomaterials for Health Care at CRIB)

  • Roman S. Polishchuk

    (Telethon Institute of Genetics and Medicine (TIGEM))

  • Daniela Corda

    (Institute of Protein Biochemistry, National Research Council)

  • Alberto Luini

    (Institute of Protein Biochemistry, National Research Council
    IRCCS SDN Istituto di Ricerca Diagnostica e Nucleare)

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).

Suggested Citation

  • Alessandro Pagliuso & Carmen Valente & Lucia Laura Giordano & Angela Filograna & Guiling Li & Diego Circolo & Gabriele Turacchio & Vincenzo Manuel Marzullo & Luigi Mandrich & Mikhail A. Zhukovsky & Fa, 2016. "Golgi membrane fission requires the CtBP1-S/BARS-induced activation of lysophosphatidic acid acyltransferase δ," Nature Communications, Nature, vol. 7(1), pages 1-15, November.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12148
    DOI: 10.1038/ncomms12148
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    Cited by:

    1. Keisuke Tabata & Vibhu Prasad & David Paul & Ji-Young Lee & Minh-Tu Pham & Woan-Ing Twu & Christopher J. Neufeldt & Mirko Cortese & Berati Cerikan & Yannick Stahl & Sebastian Joecks & Cong Si Tran & C, 2021. "Convergent use of phosphatidic acid for hepatitis C virus and SARS-CoV-2 replication organelle formation," Nature Communications, Nature, vol. 12(1), pages 1-15, December.

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