KDEL Receptor 1 Contributes to Cell Surface Association of Protein Disulfide Isomerases

• DOI: 10.33594/000000059
• Publication Date: 2019-04-08T11:12:54Z
• Authors: Anne‐Kathrin Bartels; Sascha Göttert; Christine Desel; Miriam R. Schäfer; Sebastian Krossa; Axel J. Scheidig; Joachim Grötzinger; Inken Lorenzen
• Keywords: KDEL; Transport protein

Endoplasmic reticulum (ER)-resident proteins with a C-terminal KDEL ERretention sequence are captured in the Golgi apparatus by receptors (KDELRs). The binding of such to these induces their retrograde transport. Nevertheless, some proteins, as Protein Disulfide Isomerases (PDIs), found at cell surface. PDIs target disulfide bridges extracellular domains integrins or A Disintegrin And Metalloprotease 17 (ADAM17) leading changes structure and function molecules. Integrins become activated ADAM17 inactivated upon isomerization. way that escape from transport reach plasma membrane remains far clear. Various mechanisms might exist, depending on whether local surface association more global secretion is required.To get detailed insight surface, methods biotinylation, flow cytometric analysis, immunoprecipitation, fluorescence microscopy well labeling cells labled recombinant PDIA6 was performed.Here, we show ER retention sufficient prevent into space but mandatory for its trafficking PDIA1, PDIA3, dependent KDELR1, which travels dynamic manner This assumed result PDI association, differs inducible space. Distinct differ properties. Endogenous detectable be involved not only cell-surface-associated PDIs, also retrieval internalization space.Beside motive travel Here they different render function. To via various pathways. One them depends can where it expected release cargo close vicinity Hence, needed PDIA6.