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

Alessandro Pagliuso, Carmen Valente (), Lucia Laura Giordano, Angela Filograna, Guiling Li, Diego Circolo, Gabriele Turacchio, Vincenzo Manuel Marzullo, Luigi Mandrich, Mikhail A. Zhukovsky, Fabio Formiggini, Roman S. Polishchuk, Daniela Corda () and Alberto Luini ()
Additional contact information
Alessandro Pagliuso: Institute of Protein Biochemistry, National Research Council
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
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

Nature Communications, 2016, vol. 7, issue 1, 1-15

Abstract: 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).

Date: 2016
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms12148 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms12148

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms12148

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().