Karina Reiss

TL;DR: It is demonstrated here that neuronal cadherin (N‐cadherin) is cleaved specifically by the disintegrin and metalloproteinase ADAM10 in its ectodomain, leading to the conclusion that this protease constitutes a central switch in the signalling pathway from N‐cADherin at the cell surface to β‐catenin/LEF‐1‐regulated gene expression in the nucleus.

TL;DR: It is demonstrated that dysregulated EGFR-ligand shedding may be caused by increased expression of constitutively active sheddases or activation of different sheddase by distinct stimuli, including phorbol esters and calcium influx.

TL;DR: It is demonstrated that L1 cleavage is mediated by two distinct members of the disintegrin and metalloprotease family, ADAM10 and ADAM17, both critically affecting the physiological functions of this adhesion protein.

TL;DR: Evidence is presented that Klotho is shedded by the α‐secretases ADAM10 and 17 as well as by the β‐secretase β‐APP cleaving enzyme 1, which suggests that therapeutic approaches targeting these proteases should be carefully analyzed for potential side effects on KlothO‐mediated physiological processes.