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Human prostaglandin EP3 receptor isoforms show different agonist‐induced internalization patterns
Author(s) -
Bilson Heather A,
Mitchell Deanah L,
Ashby Barrie
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.06.089
Subject(s) - internalization , receptor , prostaglandin e2 receptor , microbiology and biotechnology , gene isoform , agonist , chemistry , hek 293 cells , biology , biochemistry , gene
The human prostaglandin EP3 receptor comprises eight isoforms that differ in carboxyl‐tail. We show here that the isoforms are trafficked differently. When expressed in HEK293 cells, the isoforms located to the cell surface, although a fraction of some remained in the cell. Upon prostaglandin E 2 stimulation, EP3.I internalized almost completely, EP3.II, EP3.V, EP3.VI and EP3.f internalized to a lesser extent and EP3.III and EP3.IV did not internalize. Both EP3.I and EP3.f internalized with β‐arrestin and internalization were blocked by a dominant negative form of Eps15, a clathrin‐associated protein. Although EP3.II internalized, β‐arrestin did not translocate with the receptor and internalization was not blocked by mutant Eps15. EP3.V and EP3.VI internalized to discrete areas of the cell with β‐arrestin.