Susanne Berghöfer

TL;DR: Results obtained on furin mutants with substitutions and deletions of amino acids in the cytoplasmic tail indicate that wild‐type furin is concentrated in the TGN by a mechanism involving two independent targeting signals, which consist of the acidic peptide CPSDSEEDEG783 and the tetrapeptide YKGL765.

TL;DR: Comparative analysis with furin expressed from cDNA reveals that the truncated form prevails in preparations of biologically active, endogenous furin obtained from MDBK cells, supporting the concept that secretion of truncated furin is a physiological event that may have important implications for the processing of extracellular substrates.

TL;DR: Data is presented showing that the furin tail interacts with the medium (μ2) subunit of the AP-2 plasma membrane-specific adaptor complex in vitro and that this interaction primarily depends on recognition of the tyrosine-based sorting signal and to less extent on the leucine-isoleucine motif.

TL;DR: It is found that besides depending on the phosphorylation state of a casein kinase II site, interaction of the furin tail with AP-1 and its μ1subunit is mediated by a tyrosine motif and to less extent by a leucine-isoleucine signal, whereas a monophenylalanine motif is only involved in binding to the intactAP-1 complex.

TL;DR: In this article, a SARS-CoV-2 spike (S1) protein enzyme-linked immunosorbent assay (ELISA) was developed to detect SARS CoV2-specific antibodies.