University of Oulu

Pietilä, E. M., Tuusa, J. T., Apaja, P. M., Aatsinki, J. T., Hakalahti, A. E., Rajaniemi, H. J., & Petäjä-Repo, U. E. (2005). Inefficient Maturation of the Rat Luteinizing Hormone Receptor. Journal of Biological Chemistry, 280(28), 26622–26629. https://doi.org/10.1074/jbc.m413815200

Inefficient maturation of the rat luteinizing hormone receptor : a putative way to regulate receptor numbers at the cell surface

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Author: Pietilä, E. Maritta1; Tuusa, Jussi T.1; Apaja, Pirjo M.1;
Organizations: 1Biocenter Oulu and Department of Anatomy and Cell Biology, University of Oulu
2Department of Anatomy and Cell Biology, University of Oulu
Format: article
Version: published version
Access: open
Online Access: PDF Full Text (PDF, 0.2 MB)
Persistent link: http://urn.fi/urn:nbn:fi-fe202002064746
Language: English
Published: American Society for Biochemistry and Molecular Biology, 2005
Publish Date: 2020-02-06
Description:

Abstract

Increasing evidence suggests that the folding and maturation of monomeric proteins and assembly of multimeric protein complexes in the endoplasmic reticulum (ER) may be inefficient not only for mutants that carry changes in the primary structure but also for wild type proteins. In the present study, we demonstrate that the rat luteinizing hormone receptor, a G protein-coupled receptor, is one of these proteins that matures inefficiently and appears to be very prone to premature degradation. A substantial portion of the receptors in stably transfected human embryonic kidney 293 cells existed in immature form of Mr 73,000, containing high mannose-type N-linked glycans. In metabolic pulse-chase studies, only ∼20% of these receptor precursors were found to gain hormone binding ability and matured to a form of Mr 90,000, containing bi- and multiantennary sialylated N-linked glycans. The rest had a propensity to form disulfide-bonded complexes with a Mr 120,000 protein in the ER membrane and were eventually targeted for degradation in proteasomes. The number of membrane-bound receptor precursors increased when proteasomal degradation was inhibited, and no cytosolic receptor forms were detected, suggesting that retrotranslocation of the misfolded/incompletely folded receptors is tightly coupled to proteasomal function. Furthermore, a proteasomal blockade was found to increase the number of receptors that were capable of hormone binding. Thus, these results raise the interesting possibility that luteinizing hormone receptor expression at the cell surface may be controlled at the ER level by regulating the number of newly synthesized proteins that will mature and escape the ER quality control and premature degradation.

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Series: Journal of biological chemistry
ISSN: 0021-9258
ISSN-E: 1083-351X
ISSN-L: 0021-9258
Volume: 280
Issue: 28
Pages: 26622 - 26629
DOI: 10.1074/jbc.M413815200
OADOI: https://oadoi.org/10.1074/jbc.M413815200
Type of Publication: A1 Journal article – refereed
Field of Science: 1182 Biochemistry, cell and molecular biology
Subjects:
Copyright information: This research was originally published in the Journal of Biological Chemistry. Pietilä, E. M., Tuusa, J. T., Apaja, P. M., Aatsinki, J. T., Hakalahti, A. E., Rajaniemi, H. J., & Petäjä-Repo, U. E. (2005). Inefficient Maturation of the Rat Luteinizing Hormone Receptor. J. Biol. Chem. 2005; 280:26622-26629. © the American Society for Biochemistry and Molecular Biology.