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		<title>Several prizes in 2023 and 2024</title>
		<link>https://sites.uclouvain.be/morsommelab/2024/12/06/several-prizes-in-2023-and-2024/</link>
		
		<dc:creator><![CDATA[Pierre Morsomme]]></dc:creator>
		<pubDate>Fri, 06 Dec 2024 14:11:01 +0000</pubDate>
				<category><![CDATA[Non classé]]></category>
		<guid isPermaLink="false">https://sites.uclouvain.be/morsommelab/?p=4053</guid>

					<description><![CDATA[In 2023–2024, two Master’s students were awarded prizes for their theses. Andréa received the prestigious Adrien Bauchau Prize for the Best Master’s Thesis in the FWB and Manon received the prize for the best thesis in the BBMC Master’s program. Several prizes were also awarded to PhD students: Guillemette won the MT180 contest at UCLouvain and received the award for best oral presentation at the 2024 PhD Day; Andréa won the best poster prize at the SFMBBM meeting in 2023; and Quentin received the best poster award at the SMYTE meeting in York in 2024. Congratulations to all of you!]]></description>
										<content:encoded><![CDATA[<p data-start="47" data-end="307">In 2023–2024, two Master’s students were awarded prizes for their theses. Andréa received the prestigious Adrien Bauchau Prize for the Best Master’s Thesis in the FWB and Manon received the prize for the best thesis in the BBMC Master’s program.</p>
<p data-start="309" data-end="623">Several prizes were also awarded to PhD students: Guillemette won the MT180 contest at UCLouvain and received the award for best oral presentation at the 2024 PhD Day; Andréa won the best poster prize at the SFMBBM meeting in 2023; and Quentin received the best poster award at the SMYTE meeting in York in 2024.</p>
<p data-start="625" data-end="655" data-is-last-node="" data-is-only-node="">Congratulations to all of you!</p>
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		<title>Benjamin&#8217;s work is now published in Science Advances</title>
		<link>https://sites.uclouvain.be/morsommelab/2023/12/15/benjamins-work-is-now-published-in-science-advances/</link>
		
		<dc:creator><![CDATA[Pierre Morsomme]]></dc:creator>
		<pubDate>Fri, 15 Dec 2023 14:25:41 +0000</pubDate>
				<category><![CDATA[Non classé]]></category>
		<guid isPermaLink="false">https://sites.uclouvain.be/morsommelab/?p=4058</guid>

					<description><![CDATA[The excellent work of Benjamin on plasma membrane nanodeformations is now published in Science Advances Plasma membrane nanodeformations promote actin polymerization through CIP4/CDC42 recruitment and regulate type II IFN signaling. Ledoux B, Zanin N, Yang J, Mercier V, Coster C, Dupont-Gillain C, Alsteens D, Morsomme P, Renard HF. Sci Adv. 2023 Dec 15;9(50):eade1660. doi: 10.1126/sciadv.ade1660. Epub 2023 Dec 13. &#160;]]></description>
										<content:encoded><![CDATA[<p>The excellent work of Benjamin on plasma membrane nanodeformations is now published in Science Advances</p>
<p>Plasma membrane nanodeformations promote actin polymerization through CIP4/CDC42 recruitment and regulate type II IFN signaling.</p>
<p>Ledoux B, Zanin N, Yang J, Mercier V, Coster C, Dupont-Gillain C, Alsteens D, Morsomme P, Renard HF. Sci Adv. 2023 Dec 15;9(50):eade1660. doi: 10.1126/sciadv.ade1660. Epub 2023 Dec 13.</p>
<p>&nbsp;</p>
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		<title>GDT1 transports protons: a new publication in JBC</title>
		<link>https://sites.uclouvain.be/morsommelab/2023/04/27/gdt1-transports-protons-a-new-publication-in-jbc/</link>
		
		<dc:creator><![CDATA[Pierre Morsomme]]></dc:creator>
		<pubDate>Thu, 27 Apr 2023 14:04:40 +0000</pubDate>
				<category><![CDATA[Non classé]]></category>
		<guid isPermaLink="false">https://sites.uclouvain.be/morsommelab/?p=3983</guid>

					<description><![CDATA[Antoine Deschamps and coworkers have demonstrate that H+ ions are transported in exchange for Ca2+ and Mn2+ cations by the Golgi-localized yeast Gdt1 protein. We performed direct transport measurement across a biological membrane by expressing Gdt1p in Lactococcus lactis bacterial cells and by recording either the extracellular pH or the intracellular pH during the application of Ca2+, Mn2+ or H+ gradients. Besides, in vivo cytosolic and Golgi pH measurements were performed in Saccharomyces cerevisiae with genetically encoded pH probes targeted to those subcellular compartments. These findings have now been published in JBC. &#160;]]></description>
										<content:encoded><![CDATA[<p><img fetchpriority="high" decoding="async" class="wp-image-3973 alignleft" src="https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/Gdt1p-and-motif-copie-e1682603922322.png" alt="" width="329" height="306" srcset="https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/Gdt1p-and-motif-copie-e1682603922322.png 784w, https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/Gdt1p-and-motif-copie-e1682603922322-300x279.png 300w, https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/Gdt1p-and-motif-copie-e1682603922322-150x140.png 150w, https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/Gdt1p-and-motif-copie-e1682603922322-768x715.png 768w" sizes="(max-width: 329px) 100vw, 329px" /></p>
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<p>Antoine Deschamps and coworkers have demonstrate that H<sup>+</sup> ions are transported in exchange for Ca<sup>2+</sup> and Mn<sup>2+</sup> cations by the Golgi-localized yeast Gdt1 protein. We performed direct transport measurement across a biological membrane by expressing Gdt1p in Lactococcus lactis bacterial cells and by recording either the extracellular pH or the intracellular pH during the application of Ca<sup>2+</sup>, Mn<sup>2+</sup> or H<sup>+</sup> gradients. Besides, in vivo cytosolic and Golgi pH measurements were performed in Saccharomyces cerevisiae with genetically encoded pH probes targeted to those subcellular compartments.</p>
<p>These findings have now been published in <a href="https://www.sciencedirect.com/science/article/pii/S0021925823002703?via%3Dihub">JBC</a>.</p>
<p>&nbsp;</p>
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		<title>Congratulations to Camille for her PhD thesis</title>
		<link>https://sites.uclouvain.be/morsommelab/2023/04/04/congratulations-to-camille-for-her-phd-thesis/</link>
		
		<dc:creator><![CDATA[Pierre Morsomme]]></dc:creator>
		<pubDate>Tue, 04 Apr 2023 13:42:48 +0000</pubDate>
				<category><![CDATA[Non classé]]></category>
		<guid isPermaLink="false">https://sites.uclouvain.be/morsommelab/?p=3953</guid>

					<description><![CDATA[Bravo Camille ! After François and Benjamin you are the third PhD student of the BAR Team to obtain a PhD. Very nice collaboration between us and UNamur. Almost at the same time as your paper published in Traffic (see below): N-BAR and F-BAR proteins—endophilin-A3 and PSTPIP1—control clathrin-independent endocytosis of L1CAM &#160;]]></description>
										<content:encoded><![CDATA[<p><img decoding="async" class=" wp-image-3933 alignleft" src="https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/IMG_1842_v2.jpg" alt="" width="261" height="196" />Bravo Camille ! After François and Benjamin you are the third PhD student of the BAR Team to obtain a PhD. Very nice collaboration between us and UNamur.</p>
<p>Almost at the same time as your paper published in Traffic (see below): <em><strong>N-BAR and F-BAR proteins—endophilin-A3 and PSTPIP1—control clathrin-independent endocytosis of L1CAM</strong></em></p>
<p>&nbsp;</p>
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		<title>Discovery of a new cargo of the Endophilin A3-mediated endocytosis pathway</title>
		<link>https://sites.uclouvain.be/morsommelab/2023/03/16/discovery-of-a-new-cargo-of-endoa3-mediated-endocytosis-pathway/</link>
		
		<dc:creator><![CDATA[Pierre Morsomme]]></dc:creator>
		<pubDate>Thu, 16 Mar 2023 13:23:07 +0000</pubDate>
				<category><![CDATA[Non classé]]></category>
		<guid isPermaLink="false">https://sites.uclouvain.be/morsommelab/?p=3633</guid>

					<description><![CDATA[N-BAR and F-BAR proteins—endophilin-A3 and PSTPIP1—control clathrin-independent endocytosis of L1CAM In the current study, we focus on the endocytosis of L1CAM. This glycoprotein plays a major role in the development of the nervous system, and is involved in cancer development and is associated with metastases and poor prognosis. First, we demonstrated in our cellular context that L1CAM is mainly a clathrin-independent cargo. Second, the mechanism of L1CAM endocytosis is specifically mediated by the N-BAR domain protein endophilin-A3. Third, we discovered PSTPIP1, an F-BAR domain protein, as a novel actor in this endocytic process. This work was mainly conducted by Camille Lemaigre in collaboration with Institut Curie, University of Lund, Galecto and UNamur. See the publication here]]></description>
										<content:encoded><![CDATA[<p><img decoding="async" class="wp-image-3643 size-full alignleft" src="https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/03/Capture-decran-2023-03-16-a-14.14.58.png" alt="" width="267" height="250" /></p>
<p><em><strong>N-BAR and F-BAR proteins—endophilin-A3 and PSTPIP1—control clathrin-independent endocytosis of L1CAM</strong></em></p>
<p>In the current study, we focus on the endocytosis of L1CAM. This glycoprotein plays a major role in the development of the nervous system, and is involved in cancer development and is associated with metastases and poor prognosis. First, we demonstrated in our cellular context that L1CAM is mainly a clathrin-independent cargo. Second, the mechanism of L1CAM endocytosis is specifically mediated by the N-BAR domain protein endophilin-A3. Third, we discovered PSTPIP1, an F-BAR domain protein, as a novel actor in this endocytic process. This work was mainly conducted by Camille Lemaigre in collaboration with Institut Curie, University of Lund, Galecto and UNamur.</p>
<p>See the publication <a href="https://onlinelibrary.wiley.com/doi/10.1111/tra.12883" target="_blank" rel="noopener">here</a></p>
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		<title>Congratulations to Benjamin for his PhD thesis</title>
		<link>https://sites.uclouvain.be/morsommelab/2023/02/09/congratulations-to-benjamin-for-his-phd-thesis/</link>
		
		<dc:creator><![CDATA[Pierre Morsomme]]></dc:creator>
		<pubDate>Thu, 09 Feb 2023 09:50:51 +0000</pubDate>
				<category><![CDATA[Non classé]]></category>
		<guid isPermaLink="false">https://sites.uclouvain.be/morsommelab/?p=3853</guid>

					<description><![CDATA[Beautiful images made by Benjamin during his PhD thesis in collaboration and co-supervision with Christine Dupont, David Alsteens , Henri-François Renard and my lab. Here, using homemade fluorescent nanostructured cell culture surfaces, Benjamin investigated the role of BAR domain proteins as mechanosensors of plasma membrane geometry. Our data reveal that distinct subsets of BAR proteins bind to plasma membrane deformations in a membrane curvature radius-dependent manner. Interestingly, distinct cellular processes involving BAR domain proteins seem to be primed at these sites of high membrane curvature. We focused on one of them, the local actin cytoskeleton polymerisation. We demonstrated that membrane curvature promotes the formation of dynamic actin structures mediated by the Rho GTPase CDC42, the F-BAR protein CIP4 and the presence of PI(4,5)P2, independently of clathrin. A preprint version of the paper is visible here]]></description>
										<content:encoded><![CDATA[<p>Beautiful images made by Benjamin during his PhD thesis in collaboration and co-supervision with Christine Dupont, David Alsteens , Henri-François Renard and my lab.</p>
<p><img loading="lazy" decoding="async" class="size-full wp-image-3883 aligncenter" src="https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/02/Capture-decran-2023-04-27-a-10.50.36-1.png" alt="" width="621" height="255" srcset="https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/02/Capture-decran-2023-04-27-a-10.50.36-1.png 621w, https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/02/Capture-decran-2023-04-27-a-10.50.36-1-300x123.png 300w" sizes="auto, (max-width: 621px) 100vw, 621px" /></p>
<p>Here, using homemade fluorescent nanostructured cell culture surfaces, Benjamin investigated the role of BAR domain proteins as mechanosensors of plasma membrane geometry. Our data reveal that distinct subsets of BAR proteins bind to plasma membrane deformations in a membrane curvature radius-dependent manner. Interestingly, distinct cellular processes involving BAR domain proteins seem to be primed at these sites of high membrane curvature. We focused on one of them, the local actin cytoskeleton polymerisation. We demonstrated that membrane curvature promotes the formation of dynamic actin structures mediated by the Rho GTPase CDC42, the F-BAR protein CIP4 and the presence of PI(4,5)P2, independently of clathrin.</p>
<p>A preprint version of the paper is visible <a href="https://www.biorxiv.org/content/10.1101/2022.08.16.504113v1">here </a></p>
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		<title>Congrats to Andréa and Marie-Odile for their FRIA fellowship</title>
		<link>https://sites.uclouvain.be/morsommelab/2022/09/01/andrea-and-marie-odile-have-received-a-fria-fellowship/</link>
		
		<dc:creator><![CDATA[Pierre Morsomme]]></dc:creator>
		<pubDate>Thu, 01 Sep 2022 15:08:18 +0000</pubDate>
				<category><![CDATA[Non classé]]></category>
		<guid isPermaLink="false">https://sites.uclouvain.be/morsommelab/?p=3383</guid>

					<description><![CDATA[So nice! Marie-Odile and Andréa have obtained a FRIA fellowship to perform a PhD thesis. They will analyse the impact of TMEM165 deficiency on the cell physiology. Let&#8217;s go to new and exciting adventures full of fascinating discoveries.]]></description>
										<content:encoded><![CDATA[<p>So nice! Marie-Odile and Andréa have obtained a FRIA fellowship to perform a PhD thesis. They will analyse the impact of TMEM165 deficiency on the cell physiology. Let&rsquo;s go to new and exciting adventures full of fascinating discoveries.</p>
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		<title>Role of actin in EndoA3-mediated endocytosis of CD166</title>
		<link>https://sites.uclouvain.be/morsommelab/2022/07/16/role-of-actin-in-endoa3-mediated-endocytosis-of-cd166/</link>
		
		<dc:creator><![CDATA[Pierre Morsomme]]></dc:creator>
		<pubDate>Sat, 16 Jul 2022 11:49:57 +0000</pubDate>
				<category><![CDATA[Non classé]]></category>
		<guid isPermaLink="false">https://sites.uclouvain.be/morsommelab/?p=3553</guid>

					<description><![CDATA[In mammalian cells, we studied the way a protein called CD166 is removed from the cell surface by endocytosis. In this study, we discovered new molecular components of the mechanism that drives CD166 endocytosis. First, we observed that the skeleton of the cell, composed of actin molecules, appears to assist endophilin-A3 in the formation of the membrane pits that engulf CD166. Secondly, we discovered that the protein Rac1 orchestrates the action of actin in this process. Finally, we observed that the release of vesicles containing CD166 inside the cell is assisted by another component of the cellular skeleton – the microtubules – and motor proteins called kinesins. This work as been performed by François Tyckaert and was co-supervised by Henri-François Renard. See the full paper in Journal of Cell Science Research highlight in JCS See also a nice interview of François Tyckaert]]></description>
										<content:encoded><![CDATA[<p><img loading="lazy" decoding="async" class="alignleft" src="https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/03/Capture-decran-2023-03-16-a-13.46.59.png" alt="" width="268" height="268" />In mammalian cells, we studied the way a protein called CD166 is removed from the cell surface by endocytosis. In this study, we discovered new molecular components of the mechanism that drives CD166 endocytosis. First, we observed that the skeleton of the cell, composed of actin molecules, appears to assist endophilin-A3 in the formation of the membrane pits that engulf CD166. Secondly, we discovered that the protein Rac1 orchestrates the action of actin in this process. Finally, we observed that the release of vesicles containing CD166 inside the cell is assisted by another component of the cellular skeleton – the microtubules – and motor proteins called kinesins. This work as been performed by François Tyckaert and was co-supervised by Henri-François Renard.</p>
<p>See the full paper in <a href="https://doi.org/10.1242/jcs.259623" target="_blank" rel="noopener">Journal of Cell Science</a></p>
<p>Research highlight in <a href="https://journals.biologists.com/jcs/article/135/14/e135_e1402/276128/New-insights-into-endophilin-A3-mediated" target="_blank" rel="noopener">JCS</a></p>
<p>See also a nice interview of <a href="https://journals.biologists.com/jcs/article/135/14/jcs260401/276042/First-person-Francois-Tyckaert" target="_blank" rel="noopener">François Tyckaert</a></p>
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		<title>Congratulations to François for his PhD thesis</title>
		<link>https://sites.uclouvain.be/morsommelab/2022/06/07/congratulations-to-francois-for-his-phd-thesis/</link>
		
		<dc:creator><![CDATA[Pierre Morsomme]]></dc:creator>
		<pubDate>Tue, 07 Jun 2022 08:33:09 +0000</pubDate>
				<category><![CDATA[Non classé]]></category>
		<guid isPermaLink="false">https://sites.uclouvain.be/morsommelab/?p=3813</guid>

					<description><![CDATA[François Tyckaert is the first PhD student co-supervised by Henri-François Renard and myself. Using state-of-the-art microscopy and cell biology techniques, François could show that CD166 is a clathrin- and dynamin-independent cargo internalized via a novel endocytic mechanism that involves the BAR domain protein endophilin-A3 and the extracellular lectin galectin-8. Additionally, he could demonstrate that the actin cytoskeleton and its regulatory GTPase Rac1 dynamically associate with CD166-positive endocytic carriers and that their perturbation strongly inhibits the uptake process. He also provided evidence that microtubules and kinesin molecular motors are required to potentiate the endoA3-dependent endocytosis of CD166.]]></description>
										<content:encoded><![CDATA[<p><img loading="lazy" decoding="async" class="wp-image-3823 alignleft" src="https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/Capture-decran-2023-04-27-a-10.35.33.png" alt="" width="173" height="198" /></p>
<p>François Tyckaert is the first PhD student co-supervised by Henri-François Renard and myself.</p>
<p>Using state-of-the-art microscopy and cell biology techniques, François could show that CD166 is a clathrin- and dynamin-independent cargo internalized via a novel endocytic mechanism that involves the BAR domain protein endophilin-A3 and the extracellular lectin galectin-8. Additionally, he could demonstrate that the actin cytoskeleton and its regulatory GTPase Rac1 dynamically associate with CD166-positive endocytic carriers and that their perturbation strongly inhibits the uptake process. He also provided evidence that microtubules and kinesin molecular motors are required to potentiate the endoA3-dependent endocytosis of CD166.</p>
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		<title>Congratulations to Antoine for his PhD thesis</title>
		<link>https://sites.uclouvain.be/morsommelab/2022/02/23/congratulations-to-antoine-for-his-phd-thesis/</link>
		
		<dc:creator><![CDATA[Pierre Morsomme]]></dc:creator>
		<pubDate>Wed, 23 Feb 2022 09:05:14 +0000</pubDate>
				<category><![CDATA[Non classé]]></category>
		<guid isPermaLink="false">https://sites.uclouvain.be/morsommelab/?p=3763</guid>

					<description><![CDATA[This week Antoine presented us his elegant work on GDT1-mediated proton transport. In this thesis, a heterologous expression system using Lactococcus lactis was set up for direct H+ transport assay and a Golgi-localized pH sensor was developed for in vivo measurements in S. cerevisiae. Thanks to them, Gdt1p-mediated H+ transport activity was demonstrated. Then, Antoine looked at Gdt1p regulation. He observed that Gdt1p is rapidly downregulated as a response to extracellular Mn2+ addition and that regulation occurs both at transcriptional and post-translational levels.]]></description>
										<content:encoded><![CDATA[<p><img loading="lazy" decoding="async" class="size-thumbnail wp-image-3773 alignleft" src="https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/IMG_20220204_163057353_HDR-copie-150x150.jpg" alt="" width="150" height="150" srcset="https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/IMG_20220204_163057353_HDR-copie-150x150.jpg 150w, https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/IMG_20220204_163057353_HDR-copie-300x300.jpg 300w, https://sites.uclouvain.be/morsommelab/wp-content/uploads/2023/04/IMG_20220204_163057353_HDR-copie-75x75.jpg 75w" sizes="auto, (max-width: 150px) 100vw, 150px" /></p>
<p>This week Antoine presented us his elegant work on GDT1-mediated proton transport.</p>
<p>In this thesis, a heterologous expression system using Lactococcus lactis was set up for direct H+ transport assay and a Golgi-localized pH sensor was developed for in vivo measurements in S. cerevisiae. Thanks to them, Gdt1p-mediated H+ transport activity was demonstrated. Then, Antoine looked at Gdt1p regulation. He observed that Gdt1p is rapidly downregulated as a response to extracellular Mn2+ addition and that regulation occurs both at transcriptional and post-translational levels.</p>
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