Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?
Cellular functions are regulated by extracellular signals such as hormones, neurotransmitters, matrix ligands, and other chemical or physical stimuli. Ligand binding on its transmembrane receptor induced cell signaling and the recruitment of several interacting partners to the plasma membrane. Nowad...
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2020-04-01
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| Series: | Frontiers in Oncology |
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| Online Access: | https://www.frontiersin.org/article/10.3389/fonc.2020.00519/full |
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| author | Camille Albrecht Camille Albrecht Aline Appert-Collin Aline Appert-Collin Dominique Bagnard Dominique Bagnard Sébastien Blaise Sébastien Blaise Béatrice Romier-Crouzet Béatrice Romier-Crouzet Roman G. Efremov Roman G. Efremov Hervé Sartelet Hervé Sartelet Laurent Duca Laurent Duca Pascal Maurice Pascal Maurice Amar Bennasroune Amar Bennasroune |
| author_facet | Camille Albrecht Camille Albrecht Aline Appert-Collin Aline Appert-Collin Dominique Bagnard Dominique Bagnard Sébastien Blaise Sébastien Blaise Béatrice Romier-Crouzet Béatrice Romier-Crouzet Roman G. Efremov Roman G. Efremov Hervé Sartelet Hervé Sartelet Laurent Duca Laurent Duca Pascal Maurice Pascal Maurice Amar Bennasroune Amar Bennasroune |
| author_sort | Camille Albrecht |
| collection | DOAJ |
| description | Cellular functions are regulated by extracellular signals such as hormones, neurotransmitters, matrix ligands, and other chemical or physical stimuli. Ligand binding on its transmembrane receptor induced cell signaling and the recruitment of several interacting partners to the plasma membrane. Nowadays, it is well-established that the transmembrane domain is not only an anchor of these receptors to the membrane, but it also plays a key role in receptor dimerization and activation. Indeed, interactions between transmembrane helices are associated with specific biological activity of the proteins as cell migration, proliferation, or differentiation. Overexpression or constitutive dimerization (due notably to mutations) of these transmembrane receptors are involved in several physiopathological contexts as cancers. The transmembrane domain of tyrosine kinase receptors as ErbB family proteins (implicated in several cancers as HER2 in breast cancer) or other receptors as Neuropilins has been described these last years as a target to inhibit their dimerization/activation using several strategies. In this review, we will focus on the strategy which consists in using peptides to disturb in a specific manner the interactions between transmembrane domains and the signaling pathways (induced by ligand binding) of these receptors involved in cancer. This approach can be extended to inhibit other transmembrane protein dimerization as neuraminidase-1 (the catalytic subunit of elastin receptor complex), Discoidin Domain Receptor 1 (a tyrosine kinase receptor activated by type I collagen) or G-protein coupled receptors (GPCRs) which are involved in cancer processes. |
| first_indexed | 2024-04-12T21:46:22Z |
| format | Article |
| id | doaj.art-30391ff90a5d4e85a5ed117b0ed6e268 |
| institution | Directory Open Access Journal |
| issn | 2234-943X |
| language | English |
| last_indexed | 2024-04-12T21:46:22Z |
| publishDate | 2020-04-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Oncology |
| spelling | doaj.art-30391ff90a5d4e85a5ed117b0ed6e2682022-12-22T03:15:36ZengFrontiers Media S.A.Frontiers in Oncology2234-943X2020-04-011010.3389/fonc.2020.00519526826Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells?Camille Albrecht0Camille Albrecht1Aline Appert-Collin2Aline Appert-Collin3Dominique Bagnard4Dominique Bagnard5Sébastien Blaise6Sébastien Blaise7Béatrice Romier-Crouzet8Béatrice Romier-Crouzet9Roman G. Efremov10Roman G. Efremov11Hervé Sartelet12Hervé Sartelet13Laurent Duca14Laurent Duca15Pascal Maurice16Pascal Maurice17Amar Bennasroune18Amar Bennasroune19Université de Reims Champagne-Ardenne, Reims, FranceCNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire, MEDyC, Reims, FranceUniversité de Reims Champagne-Ardenne, Reims, FranceCNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire, MEDyC, Reims, FranceUniversité de Strasbourg, Strasbourg, FranceINSERM U1119 Biopathologie de la Myéline, Neuroprotection et Stratégies Thérapeutiques, Labex Medalis, Fédération de Médecine Translationnelle de Strasbourg, Strasbourg, FranceUniversité de Reims Champagne-Ardenne, Reims, FranceCNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire, MEDyC, Reims, FranceUniversité de Reims Champagne-Ardenne, Reims, FranceCNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire, MEDyC, Reims, FranceM. M. Shemyakin and Yu. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, RussiaHigher School of Economics, Moscow, RussiaUniversité de Reims Champagne-Ardenne, Reims, FranceCNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire, MEDyC, Reims, FranceUniversité de Reims Champagne-Ardenne, Reims, FranceCNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire, MEDyC, Reims, FranceUniversité de Reims Champagne-Ardenne, Reims, FranceCNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire, MEDyC, Reims, FranceUniversité de Reims Champagne-Ardenne, Reims, FranceCNRS UMR 7369, Matrice Extracellulaire et Dynamique Cellulaire, MEDyC, Reims, FranceCellular functions are regulated by extracellular signals such as hormones, neurotransmitters, matrix ligands, and other chemical or physical stimuli. Ligand binding on its transmembrane receptor induced cell signaling and the recruitment of several interacting partners to the plasma membrane. Nowadays, it is well-established that the transmembrane domain is not only an anchor of these receptors to the membrane, but it also plays a key role in receptor dimerization and activation. Indeed, interactions between transmembrane helices are associated with specific biological activity of the proteins as cell migration, proliferation, or differentiation. Overexpression or constitutive dimerization (due notably to mutations) of these transmembrane receptors are involved in several physiopathological contexts as cancers. The transmembrane domain of tyrosine kinase receptors as ErbB family proteins (implicated in several cancers as HER2 in breast cancer) or other receptors as Neuropilins has been described these last years as a target to inhibit their dimerization/activation using several strategies. In this review, we will focus on the strategy which consists in using peptides to disturb in a specific manner the interactions between transmembrane domains and the signaling pathways (induced by ligand binding) of these receptors involved in cancer. This approach can be extended to inhibit other transmembrane protein dimerization as neuraminidase-1 (the catalytic subunit of elastin receptor complex), Discoidin Domain Receptor 1 (a tyrosine kinase receptor activated by type I collagen) or G-protein coupled receptors (GPCRs) which are involved in cancer processes.https://www.frontiersin.org/article/10.3389/fonc.2020.00519/fulltransmembrane peptidesprotein-protein interactiontransmembrane protein dimerization inhibitioncancerspeptide delivery strategy |
| spellingShingle | Camille Albrecht Camille Albrecht Aline Appert-Collin Aline Appert-Collin Dominique Bagnard Dominique Bagnard Sébastien Blaise Sébastien Blaise Béatrice Romier-Crouzet Béatrice Romier-Crouzet Roman G. Efremov Roman G. Efremov Hervé Sartelet Hervé Sartelet Laurent Duca Laurent Duca Pascal Maurice Pascal Maurice Amar Bennasroune Amar Bennasroune Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells? Frontiers in Oncology transmembrane peptides protein-protein interaction transmembrane protein dimerization inhibition cancers peptide delivery strategy |
| title | Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells? |
| title_full | Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells? |
| title_fullStr | Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells? |
| title_full_unstemmed | Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells? |
| title_short | Transmembrane Peptides as Inhibitors of Protein-Protein Interactions: An Efficient Strategy to Target Cancer Cells? |
| title_sort | transmembrane peptides as inhibitors of protein protein interactions an efficient strategy to target cancer cells |
| topic | transmembrane peptides protein-protein interaction transmembrane protein dimerization inhibition cancers peptide delivery strategy |
| url | https://www.frontiersin.org/article/10.3389/fonc.2020.00519/full |
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