Výsledky vyhledávání - "Bouvier, M. (Michel)"

N-glycan-dependent and -independent quality control of human δ opioid receptor N-terminal variants

Autor: Lackman, J. J. (Jarkko J.), Markkanen, P. M. (Piia M. H.), Hogue, M. (Mireille), Bouvier, M. (Michel), Petäjä-Repo, U. E. (Ulla E.)

Quality control (QC) in the endoplasmic reticulum (ER) scrutinizes newly synthesized proteins and directs them either to ER export or ER-associated degradation (ERAD). Here, we demonstrate that the human δ-opioid receptor (hδOR) is subjected to ERQ

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::32834bc81cf4492540073f2df4a773c7
http://urn.fi/urn:nbn:fi-fe2019120545771

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Cys-27 variant of human delta-opioid receptor modulates maturation and cell surface delivery of Phe-27 variant via heteromerization

Autor: Leskelä, T. T. (Tarja T.), Lackman, J. J. (Jarkko J.), Vierimaa, M. M. (Miia M.), Kobayashi, H. (Hiroyuki), Bouvier, M. (Michel), Petäjä-Repo, U. E. (Ulla E.)

The important role of G protein-coupled receptor homo/heteromerization in receptor folding, maturation, trafficking, and cell surface expression has become increasingly evident. Here we investigated whether the human δ-opioid receptor (hδOR) Cys-27

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::f70d062e70fc11dfbaff3ec9dff46697
http://urn.fi/urn:nbn:fi-fe2019120445647

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Distinct subcellular localization for constitutive and agonist-modulated palmitoylation of the human delta opioid receptor

Autor: Petäjä-Repo, U. E. (Ulla E.), Hogue, M. (Mireille), Leskelä, T. T. (Tarja T.), Markkanen, P. M. (Piia M. H.), Tuusa, J. T. (Jussi T.), Bouvier, M. (Michel)

Protein palmitoylation is a reversible lipid modification that plays important roles for many proteins involved in signal transduction, but relatively little is known about the regulation of this modification and the cellular location where it occurs

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::df3bde54cfd26c8a9133f36b24340e26
http://urn.fi/urn:nbn:fi-fe2019120345523

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Newly synthesized human δ opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome

Autor: Petäjä-Repo, U. E. (Ulla E.), Hogue, M. (Mireille), Laperrière, A. (André), Bhalla, S. (Suparna), Walker, P. (Philippe), Bouvier, M. (Michel)

We have previously shown that only a fraction of the newly synthesized human δ opioid receptors is able to leave the endoplasmic reticulum (ER) and reach the cell surface (Petäjä-Repo, U. E, Hogue, M., Laperrière, A., Walker, P., and Bouvier, M.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::0d09dcca96b6e8828139dd14c7539922
http://urn.fi/urn:nbn:fi-fe202002115060

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Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human δ opioid receptor

Autor: Petäjä-Repo, U. E. (Ulla E.), Hogue, M. (Mireille), Laperrière, A. (André), Walker, P. (Philippe), Bouvier, M. (Michel)

Synthesis and maturation of G protein-coupled receptors are complex events that require an intricate combination of processes that include protein folding, post-translational modifications, and transport through distinct cellular compartments. Relati

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______2423::b3f7cdf36c071f0305381bf95532fded
http://urn.fi/urn:nbn:fi-fe202002115052

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