Skip to main content
. 2020 Jan 24;11:472. doi: 10.1038/s41467-020-14390-1

Fig. 1. Design of the setup for Light-Induced Dissociation of Adherens junctions (LInDA).

Fig. 1

a The chemically induced dimerization (CID, 1) of two different proteins or of two parts of a split variant of a protein at adherens junctions (AJ) leads to formation of functional AJs and cell compaction. The dimeric complex is cleaved with light of appropriate wavelength (350–405 nm) in subcellular regions or larger areas (2), leading to AJ dissociation and cell dissemination. b Chemical structures of the photostable dimerizer Ha-BG and Ha-TMP, and the photocleavable dimerizer Ha-pl-BG and Ha-pl-TMP. c In endogenous AJ, β-catenin facilitates the connection between E-cadherin and α-catenin. d The β-catenin binding domains of E-cadherin and α-catenin were replaced by Halo tag and SNAP tag, respectively. Addition of Ha-pl-BG induces the formation of an E-cadherin-α-catenin heterodimer; application of 350–405 nm light pulse leads to complex dissociation. e The E-cadherin receptor was split in two parts, where the cytosolic juxtamembrane domain is fused with a Halo tag and the cytosolic tail fused to a DHFR tag. Addition of Ha-pl-TMP induces the reconstitution of the receptor, the binding of β-catenin at AJs and the further recruitment of α-catenin/actin complex. The dissociation is then triggered by application of 350–405 nm light pulse.