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3. Flipper Probes for the Community

Author

Assies, Lea, primary, García-Calvo, José, additional, Piazzolla, Francesca, additional, Sanchez, Samantha, additional, Kato, Takehiro, additional, Reymond, Luc, additional, Goujon, Antoine, additional, Colom, Adai, additional, López-Andarias, Javier, additional, Straková, Karolína, additional, Mahecic, Dora, additional, Mercier, Vincent, additional, Riggi, Margot, additional, Jiménez-Rojo, Noemi, additional, Roffay, Chloé, additional, Licari, Giuseppe, additional, Tsemperouli, Maria, additional, Neuhaus, Frederik, additional, Fürstenberg, Alexandre, additional, Vauthey, Eric, additional, Hoogendoorn, Sascha, additional, Gonzalez-Gaitan, Marcos, additional, Zumbuehl, Andreas, additional, Sugihara, Kaori, additional, Gruenberg, Jean, additional, Riezman, Howard, additional, Loewith, Robbie, additional, Manley, Suliana, additional, Roux, Aurelien, additional, Winssinger, Nicolas, additional, Sakai, Naomi, additional, Pitsch, Stefan, additional, and Matile, Stefan, additional

Published
2021
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5. Flipper Probes for the Community

Author

Assies, Lea, García-Calvo, José, Piazzolla, Francesca, Sánchez, Samantha, Kato, Takehiro, Reymond, Luc, Goujon, Antoine, Colom, Adai, López-Andarias, Javier, Straková, Karolína, Mahecic, Dora, Mercier, Vincent, Riggi, Margot, Jiménez-Rojo, Noemí, Roffay, Chloé, Licari, Giuseppe, Tsemperouli, Maria, Neuhaus, Frederik, Fürstenberg, Alexandre, Vauthey, Eric, Hoogendoorn, Sascha, González-Gaitán, Marcos, Zumbuehl, Andreas, Sugihara, Kaori, Gruenberg, Jean, Riezman, Howard, Loewith, Robbie, Manley, Suliana, Roux, Aurélien, Winssinger, Nicolas, Sakai, Naomi, Pitsch, Stefan, Matile, Stefan, Assies, Lea, García-Calvo, José, Piazzolla, Francesca, Sánchez, Samantha, Kato, Takehiro, Reymond, Luc, Goujon, Antoine, Colom, Adai, López-Andarias, Javier, Straková, Karolína, Mahecic, Dora, Mercier, Vincent, Riggi, Margot, Jiménez-Rojo, Noemí, Roffay, Chloé, Licari, Giuseppe, Tsemperouli, Maria, Neuhaus, Frederik, Fürstenberg, Alexandre, Vauthey, Eric, Hoogendoorn, Sascha, González-Gaitán, Marcos, Zumbuehl, Andreas, Sugihara, Kaori, Gruenberg, Jean, Riezman, Howard, Loewith, Robbie, Manley, Suliana, Roux, Aurélien, Winssinger, Nicolas, Sakai, Naomi, Pitsch, Stefan, and Matile, Stefan

Abstract

This article describes four fluorescent membrane tension probes that have been designed, synthesized, evaluated, commercialized and applied to current biology challenges in the context of the NCCR Chemical Biology. Their names are Flipper-TR®, ER Flipper-TR®, Lyso Flipper-TR®, and Mito Flipper-TR®. They are available from Spirochrome.

Published
2021

6. Black lipid membranes: investigation of their properties and their application in the characterization of active membrane components

Author

Tsemperouli, Maria and Sugihara, Kaori

Subjects
ddc:540
Abstract

In this work, a robust platform based on black lipid membranes (BLMs) was developed for the characterization of voltage sensitive dyes (VSDs) and membrane ion transport mechanism. For this purpose, lateral BLMs where electrical measurements and fluorescence microscopy setup are combined, were first demonstrated for calibrating di-4-ANEPPS a common VSD. The advantage of the setup is 1) its flexibility in the choice of lipids and the applied voltages, 2) its high stability that enables high voltage (500 mV) application and longtime measurements, and 3) its fluorescence microscopy readout, which can be directly correlated with other fluorescence microscopy experiments using VSDs. Secondly, taking advantage of the high stability, the reported platform was used for the characterization of transport activity and ion selectivity of novel synthetic ionophores based on σ hole interactions. Finally, we also explored the dynamic and structural characteristics of the classic BLMs and we addressed the existing limitations to synchronize electrical and fluorescence recordings in such platforms.

Published
2018

12. Vesicle docking and fusion pore modulation by the neuronal calcium sensor Synaptotagmin-1

Author

Tsemperouli, Maria, Cheppali, Sudheer Kumar, Molina, Felix Rivera, Chetrit, David, Landajuela, Ane, Toomre, Derek, and Karatekin, Erdem

Abstract

Synaptotagmin-1 (Syt1) is a major calcium sensor for rapid neurotransmitter release in neurons and hormone release in many neuroendocrine cells. It possesses two tandem cytosolic C2 domains that bind calcium, negatively charged phospholipids, and the neuronal SNARE complex. Calcium binding to Syt1 triggers exocytosis, but how this occurs is not well understood. Syt1 has additional roles in docking dense core vesicles (DCV) and synaptic vesicles (SV) to the plasma membrane (PM) and in regulating fusion pore dynamics. Thus, Syt1 perturbations could affect release through vesicle docking, fusion triggering, fusion pore regulation, or a combination of these. Here, using a human neuroendocrine cell line, we show that neutralization of highly conserved polybasic patches in either C2 domain of Syt1 impairs both DCV docking and efficient release of serotonin from DCVs. Interestingly, the same mutations resulted in larger fusion pores and faster release of serotonin during individual fusion events. Thus, Syt1’s roles in vesicle docking, fusion triggering, and fusion pore control may be functionally related.

Published
2024
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14. Vesicle docking and fusion pore modulation by the neuronal calcium sensor Synaptotagmin-1.

Author

Tsemperouli M, Cheppali SK, Molina FR, Chetrit D, Landajuela A, Toomre D, and Karatekin E

Abstract

Synaptotagmin-1 (Syt1) is a major calcium sensor for rapid neurotransmitter release in neurons and hormone release in many neuroendocrine cells. It possesses two tandem cytosolic C2 domains that bind calcium, negatively charged phospholipids, and the neuronal SNARE complex. Calcium binding to Syt1 triggers exocytosis, but how this occurs is not well understood. Syt1 has additional roles in docking dense core vesicles (DCV) and synaptic vesicles (SV) to the plasma membrane (PM) and in regulating fusion pore dynamics. Thus, Syt1 perturbations could affect release through vesicle docking, fusion triggering, fusion pore regulation, or a combination of these. Here, using a human neuroendocrine cell line, we show that neutralization of highly conserved polybasic patches in either C2 domain of Syt1 impairs both DCV docking and efficient release of serotonin from DCVs. Interestingly, the same mutations resulted in larger fusion pores and faster release of serotonin during individual fusion events. Thus, Syt1's roles in vesicle docking, fusion triggering, and fusion pore control may be functionally related., Competing Interests: CONFLICT OF INTERESTS The authors declare no competing financial interests.

Published
2024
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