Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein.
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 calnex...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2019-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0210396 |
| _version_ | 1819016622671659008 |
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| author | Curtis Brandt Pamela J McFie Huyen Vu Paulos Chumala George S Katselis Scot J Stone |
| author_facet | Curtis Brandt Pamela J McFie Huyen Vu Paulos Chumala George S Katselis Scot J Stone |
| author_sort | Curtis Brandt |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-21T02:50:34Z |
| format | Article |
| id | doaj.art-b2acf3ebbbb84957951342e75ee9586c |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-21T02:50:34Z |
| publishDate | 2019-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-b2acf3ebbbb84957951342e75ee9586c2022-12-21T19:18:27ZengPublic Library of Science (PLoS)PLoS ONE1932-62032019-01-01141e021039610.1371/journal.pone.0210396Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein.Curtis BrandtPamela J McFieHuyen VuPaulos ChumalaGeorge S KatselisScot J StoneTriacylglycerol 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.https://doi.org/10.1371/journal.pone.0210396 |
| spellingShingle | Curtis Brandt Pamela J McFie Huyen Vu Paulos Chumala George S Katselis Scot J Stone Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein. PLoS ONE |
| title | Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein. |
| title_full | Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein. |
| title_fullStr | Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein. |
| title_full_unstemmed | Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein. |
| title_short | Identification of calnexin as a diacylglycerol acyltransferase-2 interacting protein. |
| title_sort | identification of calnexin as a diacylglycerol acyltransferase 2 interacting protein |
| url | https://doi.org/10.1371/journal.pone.0210396 |
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