University of Michigan Center for RNA Biomedicine ????的动态

?? Lab Spotlight: Prof. Dr. Satyajit Mayor's Lab ?? Highlighting the cutting-edge research at Prof. Dr. Satyajit Mayor's Lab at TIFR-NCBS, which focuses on Cellular Organization and Signaling. Their work advances our understanding of cell membrane dynamics and molecular interactions! ???? Led by Prof. Dr. Satyajit Mayor, the lab studies membrane organization and signaling, essential for cellular communication. This research provides insights that could reshape cell biology and microscopy. ???? ?? Key Research Highlights: ?? Local Organization of the Cell Membrane: The lab explores how molecules move within cells, revealing crucial details about membrane structure. ?? Development of Microscopic Tools: By developing innovative microscopy techniques, the lab visualizes how specific membrane domains form. ?? Dynamics of Membrane Complexes: Studying actin and myosin, the lab uncovers the composition and behavior of membrane complexes. ?? Molecular Mechanism of Endocytosis: Focusing on dynamin-independent endocytosis, the lab uses gene-level assays and RNAi screening for deeper insights. For more on their pioneering work, visit: ??(https://lnkd.in/gm9wmDyv) ??? Credits: Poster: Abhilaya Makkuva Content: Binny Bipasha Das #LabSpotlight #NGSF #CellBiology #MembraneResearch #Endocytosis #Microscopy #Innovation

?? Lab Spotlight: Prof. Dr. Satyajit Mayor's Lab ?? Highlighting the cutting-edge research at Prof. Dr. Satyajit Mayor 's Lab at TIFR-NCBS, which focuses on Cellular Organization and Signaling. Their work advances our understanding of cell membrane dynamics and molecular interactions! ???? Led by Prof. Dr. Satyajit Mayor, the lab studies membrane organization and signaling, essential for cellular communication. This research provides insights that could reshape cell biology and microscopy. ???? ?? Key Research Highlights: ?? Local Organization of the Cell Membrane: The lab explores how molecules move within cells, revealing crucial details about membrane structure. ?? Development of Microscopic Tools: By developing innovative microscopy techniques, the lab visualizes how specific membrane domains form. ?? Dynamics of Membrane Complexes: Studying actin and myosin, the lab uncovers the composition and behavior of membrane complexes. ?? Molecular Mechanism of Endocytosis: Focusing on dynamin-independent endocytosis, the lab uses gene-level assays and RNAi screening for deeper insights. For more on their pioneering work, visit: ??(https://lnkd.in/gm9wmDyv) ??? Credits: Video: Dharani Content: Aditi #LabSpotlight #NGSF #CellBiology #MembraneResearch #Endocytosis #Microscopy #Innovation

Great talk by Zach Armstrong of the Leiden Early Drug Discovery and Development (LED3) hub at the new Leiden Seminars in Biophysics and Structural Biology (L(SB)2). He gave an exciting overview of his group's work on studying sugar-modifying enzymes with chemical and structural biology https://lnkd.in/ejrs_QBP

PPS presented at the second Swedish National PI-meeting in Molecular Life Sciences ? Malin B?ckstr?m, director of PPS presented the capabilities of PPS (www.pps.gu.se/en) in protein production at the second Swedish National PI-meeting in Molecular Life Sciences in Gothenburg (https://pi-meeting.se/), November 21th and 22nd.? The meeting was jointly organized by the?Swedish Society for Biochemistry, Biophysics and Molecular Biology, SFBBM (www.sfbbm.se) and the?Swedish National Committee for Molecular Biosciences (https://lnkd.in/dtPqD7iT). The purpose of this meeting was to enable and facilitate possibilities for additional synergies and collaborations between PIs in Sweden that conduct research within the field of Molecular Life Sciences. The meeting featured short presentations of research interests from >40 PIs from all Swedish major universities as well as many opportunities for discussions and get to know each other.

Until now, the involvement of intrinsic disorder in membrane shaping processes has not been fully understood. A multidisciplinary team around Ramachandra M Bhaskara from Institute of Biochemistry II (IBC2) now reports in PNAS detailed insights into how intrinsically disordered regions (IDRs) of membrane proteins remodel cellular membranes. Focusing on the ER-phagy receptor FAM134B, they explored how membrane-anchored disordered regions behave. Through advanced computer modeling and molecular dynamics (MD) simulations, the team found that – depending on context – these highly flexible protein regions exhibit different behaviors: Driven by their conformational entropy alone, they can sense and induce membrane curvature, thereby aiding in local remodeling. However, when combined with membrane-shaping elements like the Reticulon homology domain (RHD), they amplify large-scale remodeling processes by active scaffolding. This Janus-like behavior is sequence-encoded and shared among other proteins involved in ER-phagy. It allows IDRs to boost protein clustering and accelerate the reshaping of the ER, providing a fresh perspective on their role in regulation of membrane dynamics and shaping of cellular organelles. The study was conducted in collaboration between the Bhaskara team and the groups of Ivan ?iki? from Goethe-Universit?t Frankfurt and Gerhard Hummer from Max Planck Institute of Biophysics. The work was, amongst others, supported by the @HMWK-funded cluster ENABLE and the Deutsche Forschungsgemeinschaft (DFG) - German Research Foundation-funded SFB 1177. #autophagy #ERphagy

Really interesting article!!

Until now,?the involvement of intrinsic disorder in membrane shaping processes has not been fully understood. A multidisciplinary team around?Ramachandra M Bhaskara?from?Institute of Biochemistry II (IBC2) now?reports in PNAS?detailed?insights into how intrinsically disordered regions (IDRs)?of membrane?proteins remodel cellular?membranes. Focusing on the ER-phagy receptor FAM134B, they explored how?membrane-anchored?disordered regionsbehave. Through advanced?computer modeling and molecular dynamics (MD) simulations, the team found that?–?depending on context?–?these?highly?flexible protein regions?exhibit?different?behaviors:?Driven by their conformational entropy alone, they can sense and induce membrane curvature,?thereby?aiding in?local?remodeling.?However, when combined with membrane-shaping elements like the Reticulon homology domain (RHD), they amplify large-scale remodeling processes by active scaffolding.?This Janus-like behavior?is?sequence-encoded and shared?among other proteins involved?in?ER-phagy.?It?allows IDRs to boost protein clustering and accelerate the reshaping of the ER, providing a fresh perspective on their role in?regulation of membrane dynamics and shaping of cellular organelles.?The study?was conducted in?collaboration between the Bhaskara team and the groups of?Ivan ?iki??from?Goethe-Universit?t Frankfurt and?Gerhard Hummer?at?Max Planck Institute of Biophysics.?The work was, amongst others, supported by the HMWK-funded cluster ENABLE and the Deutsche Forschungsgemeinschaft (DFG) - German Research Foundation-funded?SFB 1177. #autophagy #ERphagy

Behavior of IDRs of membrane protein through advanced computational modeling and MD Simulation.

To continue advancing collaboration among scientific disciplines, we have created the Department of Biochemistry and Biophysics, which will unite the expertise from our existing biochemistry, physiology and biophysics departments. Dr. Samara Reck-Peterson, an esteemed mechanistic cell biologist from UC San Diego, has been recruited to lead the newly formed department. “As department chair, Dr. Reck-Peterson will bring her outstanding leadership, technical expertise and skill to foster multidisciplinary research across the institution and catalyze foundational discoveries into new and improved therapies," says Weill Cornell Medicine's Dean Robert A. Harrington. Full announcement: https://bit.ly/40Gx70f

"My Journey Into Science Advocacy And Volunteering" Read new editorial by Trushar Patel, DSc, Associate Professor at The University of Lethbridge and Canada Research Chair in RNA & Protein Biophysics for CSPC's 2024 Canadian Science Policy Magazine: https://lnkd.in/gnbMefa2 #CdnSci #CSPC2024