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J Biol Chem, Vol. 274, Issue 42, 29968-29975, October 15, 1999
From the Division of Bone and Mineral Metabolism, Harvard-Thorndike
and Charles A. Dana Research Laboratories, Department of Medicine, Beth
Israel Deaconess Medical Center and Harvard Medical School, Boston,
Massachusetts 02215
Endocytosis and intracellular trafficking of the
human parathyroid hormone receptor subtype 1 (hPTH1-Rc) and its ligands
was monitored independently by real-time fluorescence microscopy in stably transfected HEK-293 cells. Complexes of fluorescence-labeled parathyroid hormone (PTH)-(1-34) agonist bound to the hPTH1-Rc internalized rapidly at 37 °C via clathrin-coated vesicles, whereas fluorescent PTH-(7-34) antagonist-hPTH1Rc complexes did not. A functional C terminus epitope-tagged receptor (C-Tag-hPTH1-Rc) was
immunolocalized to the cell membrane and, to a lesser extent, the
cytoplasm. PTH and PTH-related protein agonists stimulated C-Tag-hPTH1-Rc internalization. Relocalization to the cell membrane occurred 1 h after removal of the ligand. Endocytosis of
fluorescent PTH agonist-hPTH1-Rc complexes was blocked by the protein
kinase C (PKC) inhibitor staurosporine but not by the specific protein kinase A inhibitor
N-(2-(methylamino)ethyl)-5-isoquinoline-sulfonamide. Fluorescent PTH antagonist-hPTH1-Rc complexes were rapidly internalized after PKC activation by phorbol 12-myristate 13-acetate or thrombin, but not after stimulation of the cAMP/protein kinase A pathway by
forskolin. In cells co-expressing the hPTH1-Rc and a green fluorescent
protein-
Endocytosis of Ligand-Human Parathyroid Hormone Receptor 1 Complexes Is Protein Kinase C-dependent and Involves
-Arrestin2
REAL-TIME MONITORING BY FLUORESCENCE MICROSCOPY
-arrestin2 fusion protein (-Arr2-GFP), PTH agonists
stimulated -Arr2-GFP mobilization to the cell membrane. Subsequently, fluorescent PTH-(1-34)-hPTH1Rc complexes and
-Arr2-GFP co-localized intracellularly. In conclusion,
agonist-activated hPTH1-Rc internalization involves -arrestin
mobilization and targeting to clathrin-coated vesicles. Our results
also indicate that receptor occupancy, rather than receptor-mediated
signaling, is necessary, although not sufficient, for endocytosis of
the hPTH1-Rc. Activation of PKC, however, is absolutely required.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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