GPCRs RESEARCH TEAM
SELECTED PUBLICATIONS
Lackman, J.J., Goth, C.K., Halim, A., Vakhrushev, S.Y., Clausen, H., Petäjä-Repo, U.E. (2018) Site-specific O-glycosylation of N-terminal serine residues by polypeptide GalNAc-transferase 2 modulates human δ-opioid receptor turnover at the plasma membrane. Cell Signal. 42:184 - 193 Abstract
Goth, C.K., Tuhkanen, H.E., Khan, H., Lackman, J.J., Wang, S., Narimatsu, Y., Hansen, L.H., Overall, C.M., Clausen, H., Schjoldager, K.T., Petäjä-Repo, U.E. (2017) Site-specific O-glycosylation by polypeptide N-acetylgalactosaminyltransferase 2 (GalNAc-transferase T2) co-regulates β1-adrenergic receptor N-terminal cleavage. J. Biol. Chem. 292:4714 - 4726 Abstract
Mattila, S.O., Tuusa, J.T. and Petäjä-Repo, U.E. (2016) Parkinson's disease-associated GPR37 undergoes metalloproteinase-mediated N-terminal cleavage and ectodomain shedding. J Cell Sci. 129:1366-1377 Abstract
Lackman, J.J., Markkanen, P.M.H., Hogue, M., Bouvier, M. and Petäjä-Repo, U.E. (2014) N-glycan dependent and independent quality control of human δ opioid receptor N-terminal variants. J. Biol. Chem. 289:17830 – 17842 Abstract
Petäjä-Repo, U. E. and Lackman, J. J. (2014) Targeting opioid receptors with pharmacological chaperones. Pharmacol Res. 83:52 – 62 Abstract
Hakalahti, A. E., Khan, H., Vierimaa, M. M., Pekkala, E., Lackman, J. J., Ulvila, J., Kerkelä, R., and Petäjä-Repo, U. E. (2013) β-adrenergic agonists mediate enhancement of β1-adrenergic receptor N-terminal cleavage and stabilization in vivo and in vitro. Mol. Pharmacol. 83:1 – 3 Abstract
Leskelä, T.T., Lackman, J.L., Vierimaa, M.M., Kobayashi, H., Bouvier, M. and Petäjä-Repo, U.E. (2012) Cys27 variant of the human δ-opioid receptor modulates maturation and cell surface delivery of the Phe27 variant via heteromerization. J. Biol. Chem. 287:5008 – 5020 Abstract
Sarajärvi, T., Tuusa, J. T., Haapasalo, A., Lackman, J. J., Sormunen, R., Helisalmi, S., Roehr, J. T., Parrado, A. R., Mäkinen, P., Bertram, L., Soininen, H., Tanzi, R. E., Petäjä-Repo, U. E., and Hiltunen, M. (2011) Cysteine 27 Variant of the δ-opioid receptor affects amyloid precursor protein processing through altered endocytic trafficking. Mol. Cell Biol. 31:2326 – 2340 Abstract
Tuusa, J.T. and Petäjä-Repo, U.E. (2011) Phe27Cys polymorphism of the human delta opioid receptor predisposes cells to compromised calcium signalling. Mol. Cell Biochem. 351:173 – 181 Abstract
Martikkala, E., Rozwandowicz-Jansen, A., Hänninen, P. Petäjä-Repo, U., and Härmä, H. (2011) A homogeneous single-label time-resolved fluorescence cAMP assay. J. Biomol. Screen. 16:356 – 362 Abstract
Hakalahti, A.E:, Tapanainen, J.M., Junttila, J.M., Kaikkonen, K.S., Huikuri, H.V. and Petäjä-Repo, U.E. (2010) Association of the beta-1 adrenergic receptor carboxyl terminal variants with left ventricular hypertrophy among diabetic and non-diabetic survivors of acute myocardial infarction. Cardiovasc. Diabetol. 9:42 Abstract
Tuusa, J.T., Leskelä, T.T. and Petäjä-Repo, U.E. (2010) Human δ opioid receptor biogenesis is regulated via interactions with SERCA2b and calnexin. FEBS J. 277:2815 – 2829 Abstract
Hakalahti, A.E., Vierimaa, M.M., Lilja, M.K., Kumpula, E.-P., Tuusa, J.T. and Petäjä-Repo, U.E. (2010) Human β1-adrenergic receptor is subject to constitutive and regulated N-terminal cleavage. J. Biol. Chem. 285:28850 – 28861 Abstract
Martikkala, E., Lehmusto, M., Lilja, M., Rozwandowicz-Jansen, A., Lunden, J., Tomohiro, T., Hänninen, P., Petäjä-Repo, U. and Härmä, H. (2009) Cell-based beta2-adrenergic receptor-ligand binding assay using synthesized europium-labeled ligands and time-resolved fluorescence. Anal. Biochem. 392:103-109 Abstract
Leskelä, T.T., Markkanen, P.M.H., Alahuhta, I. A., Tuusa, J.T. and Petäjä-Repo, U.E. (2009) Phe27Cys polymorphism alters the maturation and subcellular localization of the human delta opioid receptor. Traffic 10: 116-129 Abstract
Markkanen, P.M.H. and Petäjä-Repo, U.E. (2008) N-glycan-mediated quality control in the endoplasmic reticulum is required for the expression of correctly folded delta opioid receptors at the cell surface. J. Biol. Chem. 283: 29086–29098 Abstract
Tuusa, J.T., Markkanen, P.M.H., Apaja, P.M., Hakalahti, A.E. and Petäjä-Repo, U.E. (2007) The endoplasmic reticulum Ca2+-pump SERCA2b interacts with G protein-coupled receptors and enhances their expression at the cell surface. J. Mol. Biol. 371:622-638 Abstract
Leskelä, T.T., Markkanen, P.M.H., Pietilä, E.M., Tuusa, J.T. and Petäjä-Repo, U.E. (2007) Opioid receptor pharmacological chaperones act by binding and stabilizing newly synthesized receptors in the endoplasmic reticulum. J. Biol. Chem. 282:23171-23183 Abstract
Petäjä-Repo, U.E., Hogue, M., Leskelä, T.T., Markkanen, P.M.H., Tuusa, J.T. and Bouvier, M. (2006) Distinct subcellular localization for constitutive and agonist-modulated palmitoylation of the human delta opioid receptor. J. Biol. Chem. 281:15780-15789 Abstract
Apaja, P.M., Tuusa, J.T., Pietilä, E.M., Rajaniemi, H.J. and Petäjä-Repo, U.E. (2006) Luteinizing hormone receptor ectodomain splice variant misroutes the full-length receptor into a subcompartment of the endoplasmic reticulum. Mol. Biol. Cell 17:2243-2255 Abstract
Apaja, P.M., Aatsinki, J.T., Rajaniemi, H.J. and Petäjä-Repo, U.E. (2005) Expression of the mature luteinizing hormone receptor in rodent urogenital and adrenal tissues is developmentally regulated at a post-translational level. Endocrinology 146:3224-3232 Abstract
Pietilä, E.M., Tuusa, J.T., Apaja, P.M., Aatsinki, J.T., Hakalahti, A.E., Rajaniemi, H. J. and Petäjä-Repo, U.E. (2005) Inefficient processing of the luteinizing hormone receptor: A putative way to regulate receptor numbers at the cell surface. J. Biol. Chem. 280:26622-26629 Abstract
Apaja, P.M., Harju, K.T., Aatsinki, J.T., Petäjä-Repo, U.E. and Rajaniemi, H.J. (2004) Identification and structural characterization of the neuronal luteinizing hormone receptor associated with sensory systems. J. Biol. Chem. 279:1899-1906 Abstract
Salahpour, A., Bonin, H., Bhalla, S., Petäjä-Repo, U. and Bouvier, M. (2003) Biochemical characterization of beta2-adrenergic receptor dimers and oligomers. Biol. Chem. 384:117-123 Abstract
Petäjä-Repo, U.E., Hogue, M., Bhalla, S., Laperrière, A., Morello, J-.P., and Bouvier, M. (2002) Ligands act as pharmacological chaperones and increase the efficiency of the delta opioid receptor maturation. EMBO J. 21: 1628-1637 Abstract
Morello, J.-P., Salahpour, A., Petäjä-Repo, U.E., Laperrière, A., Lonergan, M., Arthus, M.-F., Nabi, I.R., Bichet, D.G. and Bouvier, M. (2001) Association of calnexin with wild type and mutant AVPR2 that cause nephrogenic diabetes insipidus. Biochemistry 40: 6766 - 6775 Abstract
Petäjä-Repo, U.E., Hogue, M., Laperrière, A., Bhalla, S., Walker, P. and Bouvier, M (2001) Newly synthesized human delta opioid receptors retained in the endoplasmic reticulum are retrotranslocated to the cytosol, deglycosylated, ubiquitinated, and degraded by the proteasome. J. Biol. Chem. 276: 4416 - 4423 Abstract
Morello, J.-P., Petäjä-Repo, U.E., Bichet, D.G., and Bouvier, M. (2000) Pharmacological chaperones: a new twist on receptor folding. Trends Pharmacol. Sci. 21: 466 - 469 Abstract
Petäjä-Repo, U.E., Hogue, M., Laperrière, A., Walker, P. and Bouvier, M. (2000) Export from the endoplasmic reticulum represents the limiting step in the maturation and cell surface expression of the human delta opioid receptor. J. Biol. Chem. 275: 13727 - 13736 Abstract
Morello, J-.P., Salahpour, A., Laperrière, A., Bernier, V., Arthus, M-.F., Lonergan, M., Petäjä-Repo, U.E., Angers, S., Morin, D., Bichet, D.G. and Bouvier, M. (2000) Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants. J. Clin Invest. 105: 887 - 895 Abstract