Journal
NATURE COMMUNICATIONS
Volume 7, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/ncomms12148
Keywords
-
Categories
Funding
- Italian Association for Cancer Research [IG10341, 14675, IG15767]
- MIUR [PON01-00117, PON01-00862]
- PNR-CNR Aging Program
- NanoMax
- FaReBio di Qualita
- 'Creme Campania Research in Experimental Medicine Project' POR Campania FSE, POR project OcKey
- Italian Foundation for Cancer Research Fellowships (FIRC, Milan, Italy)
Ask authors/readers for more resources
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 PI4KIIIb through a 14-3-3 gamma 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 delta (LPAAT delta) 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).
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available