Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain

The endoplasmic reticulum (ER) is equipped with protein disulfide isomerases (PDIs), molecular chaperons, and other folding enzymes to ensure that newly synthesized proteins in the ER are properly folded. Molecular chaperons and PDIs can form complex to promote protein folding in the ER of mammalian cells. In plants, many PDIs associate with each other and function cooperatively in oxidative protein folding. As a plant unique protein disulfide isomerase, Arabidopsis thaliana PDI11 (AtPDI11) demonstrates oxidative protein folding activities and works synergistically with AtPDI2/5. However, whether AtPDI11 associates with molecular chaperons or AtPDIs in catalyzing disulfide formation remained unknown. Here, we find that AtPDI11 interacts with ER resident lectin chaperones calreticulin 1 (CRT1) and CRT2. Furthermore, the D domain, but not the a or a' domain of AtPDI11 provides the biding sites for its interaction with CRT1/2. Moreover, the P domain of CRT1 is responsible for its interaction with AtPDI11. Our work implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist the folding of glycoproteins in the ER. (c) 2021 Elsevier Inc. All rights reserved.

Automated summary

The endoplasmic reticulum is equipped with protein disulfide isomerases, molecular chaperons, and other folding enzymes to ensure proper folding of newly synthesized proteins. Arabidopsis thaliana PDI11 interacts with ER resident lectin chaperones CRT1 and CRT2, with the D domain providing binding sites for this interaction. This implies that Arabidopsis CRT1/2 may specifically recruit AtPDI11 to assist in glycoprotein folding in the ER.