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Interorganellar Phosphatidylserine Transfer by Sec14 Family Protein Sfh1 in Saccharomyces cerevisiae
Author(s) -
Mizuike Aya,
Kobayashi Shingo,
Horiuchi Hiroyuki,
Ohta Akinori,
Fukuda Ryouichi
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.814.4
Subject(s) - phospholipid transfer protein , golgi apparatus , phosphatidylserine , saccharomyces cerevisiae , phospholipid , membrane contact site , microbiology and biotechnology , endoplasmic reticulum , endosome , biochemistry , yeast , chemistry , biology , membrane , membrane protein , integral membrane protein , cell
Interorganellar phospholipid transfer is critical for the generation and maintenance of uneven distribution of phospholipids in membranes and for the phospholipid synthesis through CDP‐DAG pathway in the yeast Saccharomyces cerevisiae . While involvement of lipid transfer proteins (LTPs) in directional lipid transport has been actively discussed, the precise mechanisms of interorganellar phospholipid transfer remain unsolved. We carried out a screening to identify genes involved in aminophospholipid transfer in Psd2 branch of the CDP‐DAG pathway and obtained SFH1 , a SEC14 homolog. Overexpression of SFH1 recovered the growth of psd1 Δ on non‐fermenting carbon sources without ethanolamine supplementation, and partially restored the mitochondrial and cellular PE levels. Sfh1 was able to transfer fluorescence‐labeled phosphatidylserine (PS) between liposomes in vitro . In addition, binding of Sfh1 to PS in vivo was suggested by the analysis of phospholipid species copurified with Sfh1 from yeast cells by ESI‐MS/MS. Subcellular fractionation suggested that a portion of Sfh1 is localized in the endosome and the Golgi where Psd2 is reported to be localized. Together with the results that overexpression of SFH1 did not affect the protein abundance of Pss1 and Psd2, or the in vitro Psd2 activity, it is conceivable that Sfh1 enhance PE synthesis by PS transfer from the endoplasmic reticulum to the endosome. Our findings propose a novel function for Sec14‐family proteins in yeast. Support or Funding Information This work was partly supported by JSPS KAKENHI Grant Number 17K07710 and 15J10871. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .