TY  - JOUR
AU  - Mavri, Maša
AU  - Glišić, Sanja
AU  - Senćanski, Milan
AU  - Vrecl, Milka
AU  - Rosenkilde, Mette M.
AU  - Spiess, Katja
AU  - Kubale, Valentina
PY  - 2023
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/10682
AB  - The viral G-protein-coupled receptor (vGPCR) BILF1 encoded by the Epstein–Barr virus (EBV) is an oncogene and immunoevasin and can downregulate MHC-I molecules at the surface of infected cells. MHC-I downregulation, which presumably occurs through co-internalization with EBV-BILF1, is preserved among BILF1 receptors, including the three BILF1 orthologs encoded by porcine lymphotropic herpesviruses (PLHV BILFs). This study aimed to understand the detailed mechanisms of BILF1 receptor constitutive internalization, to explore the translational potential of PLHV BILFs compared with EBV-BILF1.
T2  - Cellular and Molecular Biology Letters
T1  - Patterns of human and porcine gammaherpesvirus-encoded BILF1 receptor endocytosis
VL  - 28
IS  - 1
SP  - 14
DO  - 10.1186/s11658-023-00427-y
ER  - 

@article{
author = "Mavri, Maša and Glišić, Sanja and Senćanski, Milan and Vrecl, Milka and Rosenkilde, Mette M. and Spiess, Katja and Kubale, Valentina",
year = "2023",
abstract = "The viral G-protein-coupled receptor (vGPCR) BILF1 encoded by the Epstein–Barr virus (EBV) is an oncogene and immunoevasin and can downregulate MHC-I molecules at the surface of infected cells. MHC-I downregulation, which presumably occurs through co-internalization with EBV-BILF1, is preserved among BILF1 receptors, including the three BILF1 orthologs encoded by porcine lymphotropic herpesviruses (PLHV BILFs). This study aimed to understand the detailed mechanisms of BILF1 receptor constitutive internalization, to explore the translational potential of PLHV BILFs compared with EBV-BILF1.",
journal = "Cellular and Molecular Biology Letters",
title = "Patterns of human and porcine gammaherpesvirus-encoded BILF1 receptor endocytosis",
volume = "28",
number = "1",
pages = "14",
doi = "10.1186/s11658-023-00427-y"
}

Mavri, M., Glišić, S., Senćanski, M., Vrecl, M., Rosenkilde, M. M., Spiess, K.,& Kubale, V.. (2023). Patterns of human and porcine gammaherpesvirus-encoded BILF1 receptor endocytosis. in Cellular and Molecular Biology Letters, 28(1), 14.
https://doi.org/10.1186/s11658-023-00427-y

Mavri M, Glišić S, Senćanski M, Vrecl M, Rosenkilde MM, Spiess K, Kubale V. Patterns of human and porcine gammaherpesvirus-encoded BILF1 receptor endocytosis. in Cellular and Molecular Biology Letters. 2023;28(1):14.
doi:10.1186/s11658-023-00427-y .

Mavri, Maša, Glišić, Sanja, Senćanski, Milan, Vrecl, Milka, Rosenkilde, Mette M., Spiess, Katja, Kubale, Valentina, "Patterns of human and porcine gammaherpesvirus-encoded BILF1 receptor endocytosis" in Cellular and Molecular Biology Letters, 28, no. 1 (2023):14,
https://doi.org/10.1186/s11658-023-00427-y . .

TY  - JOUR
AU  - Susec, Maja
AU  - Senćanski, Milan V.
AU  - Glišić, Sanja
AU  - Veljković, Nevena V.
AU  - Pedersen, Christina
AU  - Drinovec, Luka
AU  - Stojan, Jurij
AU  - Nøhr, Jane
AU  - Vrecl, Milka
PY  - 2019
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/8490
AB  - This study aimed to functionally characterize β2-adrenergic (β2AR) and insulin receptor (IR) heteromers in regard to β-arrestin 2 (βarr2) recruitment and cAMP signaling and to examine the involvement of the cytoplasmic portion of the IR β chain in heteromerization with β2AR. Evidence for β2AR:IR:βarr2 complex formation and the specificity of the IR:βarr2 interaction was first provided by bioinfomatics analysis. Receptor-heteromer investigation technology (HIT) then provided functional evidence of β2AR:IR heterodimerization by showing isoproterenol-induced but not insulin-induced GFP2-βarr2 recruitment to the β2AR:IR complex; the IR:βarr2 interaction was found to only be constitutive. The constitutive IR:βarr2 BRET signal (BRETconst) was significantly smaller in cells coexpressing IR-RLuc8 and a GFP2-βarr2 1–185 mutant lacking the proposed IR binding domain. β2AR:IR heteromerization also influenced the pharmacological phenotype of β2AR, i.e., its efficacy in recruiting βarr2 and activating cAMP signaling. Evidence suggesting involvement of the cytoplasmic portion of the IR β chain in the interaction with β2AR was provided by BRET2 saturation and HIT assays using an IR 1–1271 stop mutant lacking the IR C-terminal tail region. For the complex consisting of IR 1–1271–RLuc8:β2AR-GFP2, saturation was not reached, most likely reflecting random collisions between IR 1–1271 and β2AR. Furthermore, in the HIT assay, no substantial agonist-induced increase in the BRET2 signal was detected that would be indicative of βarr2 recruitment to the IR 1–1271:β2AR heteromer. Complementary 3D visualization of β2AR:IR provided supporting evidence for stability of the heterotetramer complex and identified amino acid residues involved in β2AR:IR heteromerization. © 2019
T2  - Neuropharmacology
T1  - Functional characterization of β2-adrenergic and insulin receptor heteromers
VL  - 152
SP  - 78
EP  - 89
DO  - 10.1016/j.neuropharm.2019.01.025
ER  - 

@article{
author = "Susec, Maja and Senćanski, Milan V. and Glišić, Sanja and Veljković, Nevena V. and Pedersen, Christina and Drinovec, Luka and Stojan, Jurij and Nøhr, Jane and Vrecl, Milka",
year = "2019",
abstract = "This study aimed to functionally characterize β2-adrenergic (β2AR) and insulin receptor (IR) heteromers in regard to β-arrestin 2 (βarr2) recruitment and cAMP signaling and to examine the involvement of the cytoplasmic portion of the IR β chain in heteromerization with β2AR. Evidence for β2AR:IR:βarr2 complex formation and the specificity of the IR:βarr2 interaction was first provided by bioinfomatics analysis. Receptor-heteromer investigation technology (HIT) then provided functional evidence of β2AR:IR heterodimerization by showing isoproterenol-induced but not insulin-induced GFP2-βarr2 recruitment to the β2AR:IR complex; the IR:βarr2 interaction was found to only be constitutive. The constitutive IR:βarr2 BRET signal (BRETconst) was significantly smaller in cells coexpressing IR-RLuc8 and a GFP2-βarr2 1–185 mutant lacking the proposed IR binding domain. β2AR:IR heteromerization also influenced the pharmacological phenotype of β2AR, i.e., its efficacy in recruiting βarr2 and activating cAMP signaling. Evidence suggesting involvement of the cytoplasmic portion of the IR β chain in the interaction with β2AR was provided by BRET2 saturation and HIT assays using an IR 1–1271 stop mutant lacking the IR C-terminal tail region. For the complex consisting of IR 1–1271–RLuc8:β2AR-GFP2, saturation was not reached, most likely reflecting random collisions between IR 1–1271 and β2AR. Furthermore, in the HIT assay, no substantial agonist-induced increase in the BRET2 signal was detected that would be indicative of βarr2 recruitment to the IR 1–1271:β2AR heteromer. Complementary 3D visualization of β2AR:IR provided supporting evidence for stability of the heterotetramer complex and identified amino acid residues involved in β2AR:IR heteromerization. © 2019",
journal = "Neuropharmacology",
title = "Functional characterization of β2-adrenergic and insulin receptor heteromers",
volume = "152",
pages = "78-89",
doi = "10.1016/j.neuropharm.2019.01.025"
}

Susec, M., Senćanski, M. V., Glišić, S., Veljković, N. V., Pedersen, C., Drinovec, L., Stojan, J., Nøhr, J.,& Vrecl, M.. (2019). Functional characterization of β2-adrenergic and insulin receptor heteromers. in Neuropharmacology, 152, 78-89.
https://doi.org/10.1016/j.neuropharm.2019.01.025

Susec M, Senćanski MV, Glišić S, Veljković NV, Pedersen C, Drinovec L, Stojan J, Nøhr J, Vrecl M. Functional characterization of β2-adrenergic and insulin receptor heteromers. in Neuropharmacology. 2019;152:78-89.
doi:10.1016/j.neuropharm.2019.01.025 .

Susec, Maja, Senćanski, Milan V., Glišić, Sanja, Veljković, Nevena V., Pedersen, Christina, Drinovec, Luka, Stojan, Jurij, Nøhr, Jane, Vrecl, Milka, "Functional characterization of β2-adrenergic and insulin receptor heteromers" in Neuropharmacology, 152 (2019):78-89,
https://doi.org/10.1016/j.neuropharm.2019.01.025 . .