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J Biol Chem, Vol. 275, Issue 12, 8664-8671, March 24, 2000

Subtype-specific Trafficking of Endothelin Receptors*

Yoichiro AbeDagger , Kazuhisa Nakayama§, Akihiro Yamanaka, Takeshi Sakurai, and Katsutoshi Goto

From the Department of Pharmacology, Institute of Basic Medical Sciences and § Institute of Biological Sciences and Gene Experiment Center, University of Tsukuba, Tsukuba, Ibaraki 305-8575, Japan

We investigated the subcellular localization of two endothelin receptors (ETAR and ETBR). To visualize these receptors directly, the C terminus of each receptor was fused to the N terminus of enhanced green fluorescent protein (designated as ETR-EGFP). When transiently expressed in various mammalian cell lines, ETAR-EGFP was predominantly localized on the plasma membrane. By contrast, ETBR-EGFP was, independent of ligand stimulation, predominantly localized on the intracellular vesicular structures containing Lamp-1. Immunoblot analyses revealed that at steady state ETBR-EGFP was highly degraded, and its degradation was inhibited by bafilomycin A1. Antibody uptake experiments suggested that the ETBR-EGFP molecules were internalized from the plasma membrane. It is therefore likely that ETBR is first transported to the plasma membrane and then internalized, irrespective of ligand stimulation, to lysosomes where it undergoes proteolytic degradation. Exchanging the C-terminal cytoplasmic tails of the two ETRs revealed that the cytoplasmic tail is responsible for both the intracellular localization and the degradation of the receptors. Deletion of the extreme C-terminal 35 amino acids from both receptors allowed the receptor proteins to localize predominantly in the intracellular vesicles and to degrade. These observations indicate that the cytoplasmic tail of ETAR determines its plasma membrane localization. Stimulation with endothelin-1 increased the amount of intact ETR-EGFP fusion proteins without increasing their de novo synthesis, suggesting that binding of endothelin-1 stabilizes the ETRs.

* This work was supported in part by research grants from the Ministry of Education, Science and Culture of Japan, from the University of Tsukuba Research Project, and from the Japan Society for the Promotion of Science (JSPS-RFTF96I00202).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Present address: Dept. of Pharmacology and Neuroscience, KEIO University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan.

To whom correspondence should be addressed: Dept. of Pharmacology, Institute of Basic Medical Sciences, University of Tsukuba, Tsukuba, Ibaraki 305-8575, Japan. Tel.: 81-298-53-3277; Fax: 81-298-53-3039; E-mail: kgoto@md.tsukuba.ac.jp.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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