Ontology highlight
ABSTRACT:
SUBMITTER: Klenk C
PROVIDER: S-EPMC2838289 | biostudies-literature | 2010 Mar
REPOSITORIES: biostudies-literature
Klenk Christoph C Schulz Stefan S Calebiro Davide D Lohse Martin J MJ
The Journal of biological chemistry 20100115 12
The receptor for parathyroid hormone (PTHR) is a main regulator of calcium homeostasis and bone maintenance. As a member of class B of G protein-coupled receptors, it harbors a large extracellular domain, which is required for ligand binding. Here, we demonstrate that the PTHR extracellular domain is cleaved by a protease belonging to the family of extracellular metalloproteinases. We show that the cleavage takes place in a region of the extracellular domain that belongs to an unstructured loop ...[more]