Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 493, Issue 1, Pages 202-206Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2017.09.046
Keywords
Fabp5; Calnexin; Endoplasmic reticulum
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Funding
- Alberta MS Network
- Canadian Institutes of Health Research [MOP-15291, MOP-15415, MOP-86750, PS-153325]
- Natural Sciences and Engineering Research Council of Canada [2015-04390]
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Calnexin is a type 1 integral endoplasmic reticulum membrane molecular chaperone with an endoplasmic reticulum luminal chaperone domain and a highly conserved C-terminal domain oriented to the cytoplasm. Fabp5 is a cytoplasmic protein that binds long-chain fatty acids and other lipophilic ligands. Using a yeast two-hybrid screen, immunoprecipitation, microscale thermophoresis analysis and cellular fractionation, we discovered that Fabp5 interacts with the calnexin cytoplasmic C-tail domain at the endoplasmic reticulum. These observations identify Fabp5 as a previously unrecognized calnexin binding partner. (C) 2017 Elsevier Inc. All rights reserved.
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