Transmembrane association of DDR1 and DDR2 mediated by Leucine zipper motifs.

ABSTRACT: Discoidin domain receptors (DDRs) are single-pass transmembrane proteins belonging to receptor tyrosine kinases (RTKs) family, which are activated by collagen ligands with unusual slow, sustained kinetics, distinguishing them from canonical RTKs. While DDRs play critical roles in cell adhesion, differentiation, and cancer progression, their activation mechanisms remain partly understood. Here, we investigated the transmembrane domains (TMDs) of DDR1 and DDR2 to elucidate their interaction dynamics in membrane. Using bacterial adenylate cyclase two-hybrid (BACTH) assays, we demonstrated robust homotypic interactions and even stronger heterotypic associations between DDRTMDs. NMR spectroscopy of DDR1TMD and DDR2TMD reconstituted in lipid bilayer-mimetic bicelles showed obvious chemical shift

SUBMITTER: Huang F 

PROVIDER: S-EPMC12640037 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature