PLoS ONE (Jan 2019)

Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein.

  • Curtis Brandt,
  • Pamela J McFie,
  • Huyen Vu,
  • Paulos Chumala,
  • George S Katselis,
  • Scot J Stone

DOI
https://doi.org/10.1371/journal.pone.0210396
Journal volume & issue
Vol. 14, no. 1
p. e0210396

Abstract

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Triacylglycerol synthesis is catalyzed by acyl CoA:diacylglycerol acyltransferase-2 (DGAT2). DGAT2 is an integral membrane protein that is localized to the endoplasmic reticulum and interacts with lipid droplets. Using BioId, a method to detect proximal and interacting proteins, we identified calnexin as a DGAT2-interacting protein. Co-immunoprecipitation and proximity ligation assays confirmed this finding. We found that calnexin-deficient mouse embryonic fibroblasts had reduced intracellular triacylglycerol levels and fewer large lipid droplets (>1.0 μm2 area). Despite the alterations in triacylglycerol metabolism, in vitro DGAT2 activity, localization and protein stability were not affected by the absence of calnexin.