Both calcium-sensing receptor intracellular C-terminal domains support homodimer signaling.

ABSTRACT: Extracellular calcium-sensing receptors (CaSRs) are required for whole-body calcium homeostasis and operate as homodimers, shown structurally to bind only one heterotrimeric G protein at a time. Whether the intracellular domain (ICD) of the other, uncoupled monomer is functionally redundant or still required for optimal CaSR signaling remains unknown. Cotransfection of human embryonic kidney 293 cells with receptors containing both extracellular (CaSR₁^S170A) and intracellular (CaSR₂^F801A) mutations, which are nonfunctional when transfected individually, partially rescues function via trans-activation in CaSR₁^S170A:CaSR₂^F801A heterodimers. Further, mutation of an inhibitory, intracellular protein kinase

SUBMITTER: Binmahfouz LS 

PROVIDER: S-EPMC12799464 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature