MP
Structure of the Outer Membrane Transporter FemA and Its Role in the Uptake of Ferric Dihydro-Aeruginoic Acid and Ferric Aeruginoic Acid in Pseudomonas aeruginosa.
Will V, Moynié L, Si Ahmed Charrier E, Le Bas A, Kuhn L, Volck F, Chicher J, Aksoy H, Madec M, Antheaume C, Mislin GLA, Schalk IJ.
ACS Chem Biol. 2025 Mar 21;20(3):690-706.
doi: 10.1021/acschembio.4c00820. Epub 2025 Mar 4.
PMID: 40035455.
X-ray crystal structure of the OM transporter FemA from P. aeruginosa.
FemA is shown to be involved in the uptake of two siderophores: ferric dihydro-aeruginoic acid and ferric aeruginoic acid.
=> conserved binding pocket and potential gating mechanism for iron uptake.
Transporter excess and clustering facilitate adaptor protein shuttling for bacterial efflux.
Zhang W, Harper CE, Lee J, Fu B, Ramsukh M, Hernandez CJ, Chen P.
Cell Rep Phys Sci. 2025 Feb 19;6(2):102441.
doi: 10.1016/j.xcrp.2025.102441. Epub 2025 Feb 12.
PMID: 40083904.
Authors explore how bacterial efflux systems are regulated through spatial organization and MacAB TolC dynamics.
=> excess membrane transporters form clusters that enhance the recruitment and shuttling of adaptor proteins. This spatial arrangement boosts the efficiency of drug efflux.
The study suggests that transporter abundance and localization are critical for adaptive resistance mechanisms.
Cryo-EM structure of the human monocarboxylate transporter 10.
Bågenholm V, Nordlin KP, Pasquadibisceglie A, Belinskiy A, Holm CM, Hotiana HA, Gotfryd K, Delemotte L, Nour-Eldin HH, Pedersen PA, Gourdon P.
Structure. 2025 Mar 17:S0969-2126(25)00065-6.
doi: 10.1016/j.str.2025.02.012. Online ahead of print.
PMID: 40112803.
First cryo-EM structure of human MCT10, a monocarboxylate transporter responsible for shuttling aromatic amino acids.
=> substrate-binding pockets and conformational states indicative of an alternating access mechanism.
MD => residues involved in ligand specificity and proton coupling.
Learning transition path and membrane topological signatures in the folding pathway of bacteriorhodopsin (BR) fragment with artificial intelligence.
Chatterjee H, Dutta P, Zacharias M, Sengupta N.
J Chem Phys. 2025 Mar 14;162(10):104110.
doi: 10.1063/5.0250082.
PMID: 40067008.
AI to simulate the folding pathway of a BR fragment in a membrane environment.
ML models capture folding intermediates and transitions with associated membrane features.
The study identifies crucial steps in achieving native structure and membrane insertion.
Membrane drug transporters in cancer: From chemoresistance mechanism to therapeutic strategies.
Pan C, Lee LTO.
Biochim Biophys Acta Rev Cancer. 2025 Apr;1880(2):189272.
doi: 10.1016/j.bbcan.2025.189272. Epub 2025 Jan 23.
PMID: 39863184.
Review focusing on membrane transporters involved in cancer drug resistance.
Authors discuss emerging strategies to target these transporters for improved therapy.
Modeling the different conformations of the human mitochondrial ADP/ATP carrier using AlphaFold and molecular dynamics simulations of the protein-ligand complexes.
Quadrotta V, Polticelli F.
Comput Struct Biotechnol J. 2025 Mar 24;27:1265-1277.
doi: 10.1016/j.csbj.2025.03.036. eCollection 2025.
PMID: 40225838.
AF predictions + MD => model of conformational states of the mitochondrial ADP/ATP carrier.
Authors simulate transitions between matrix- and cytosol-facing states in ligand-bound complexes.
Key structural determinants of nucleotide binding and translocation are identified.
Dissecting Large-Scale Structural Transitions in Membrane Transporters Using Advanced Simulation Technologies.
Pant S, Dehghani-Ghahnaviyeh S, Trebesch N, Rasouli A, Chen T, Kapoor K, Wen PC, Tajkhorshid E.
J Phys Chem B. 2025 Apr 17;129(15):3703-3719. doi: 10.1021/acs.jpcb.5c00104. Epub 2025 Mar 18.
PMID: 40100959.
Advanced simulation methods => study of the large conformational transitions in membrane transporter function.
Authors analyze transport cycles across several families, identifying common patterns in energy landscapes and gating.
=> shows how lipid interactions modulate transport efficiency.
Ligand-Based Drug Discovery Leveraging State-of-the-Art Machine Learning Methodologies Exemplified by Cdr1 Inhibitor Prediction.
Trinh TC, Falson P, Tran-Nguyen VK, Boumendjel A.
J Chem Inf Model. 2025 Apr 16.
doi: 10.1021/acs.jcim.5c00374. Online ahead of print.
PMID: 40241349.
ML to discover inhibitors for Cdr1, a fungal drug transporter linked to antifungal resistance.
=> predictive models based on ligand features and validation through docking and biochemical assays.
=> new candidates with inhibitory activity.
Proteorhodopsin insights into the molecular mechanism of vectorial proton transport.
Bukhdruker S, Gushchin I, Shevchenko V, Kovalev K, Polovinkin V, Tsybrov F, Astashkin R, Alekseev A, Mikhaylov A, Bukhalovich S, Bratanov D, Ryzhykau Y, Kuklina D, Caramello N, Rokitskaya T, Antonenko Y, Rulev M, Stoev C, Zabelskii D, Round E, Rogachev A, Borshchevskiy V, Ghai R, Bourenkov G, Zeghouf M, Cherfils J, Engelhard M, Chizhov I, Rodriguez-Valera F, Bamberg E, Gordeliy V.
Sci Adv. 2025 Apr 18;11(16):eadu5303.
doi: 10.1126/sciadv.adu5303. Epub 2025 Apr 16.
PMID: 40238873.
This structural study elucidates how proteorhodopsin transports protons across membranes in a vectorial manner.
=> conformational shifts that couple light absorption to proton translocation.
Spectroscopy and mutagenesis support a stepwise mechanism involving key residues.
Membrane
Lipid Dynamics at Membrane Contact Sites.
Reinisch KM, De Camilli P, Melia TJ.
Annu Rev Biochem. 2025 Mar 11. doi: 10.1146/annurev-biochem-083024-122821. Online ahead of print.
PMID: 40067957.
Review exploring how lipids are transferred and remodeled at membrane contact sites between organelles.
Authors describe protein tethers and lipid transport mechanisms that coordinate membrane identity and signaling. Lipid movement at these junctions supports functions such as organelle biogenesis, calcium signaling, and metabolism.
Membrane tubulation induced by a bacterial glycolipid.
Nomura K, Tsuji A, Yamashita H, Abe M, Fujikawa K, Mori S, Osawa T, Toyonaga H, Osugi T, Yasuhara K, Morigaki K, Nishiyama KI, Shimamoto K.
Sci Rep. 2025 Mar 20;15(1):9699.
doi: 10.1038/s41598-025-93563-8.
PMID: 40113929.
A specific bacterial glycolipid can induce tubule formation in synthetic lipid bilayers.
Microscopy and biophysical assays => showh how lipid curvature and phase behavior drive membrane remodeling. These tubules mimic bacterial OMV.
Insights into lipid-driven membrane architecture changes in host-pathogen interactions.
Membrane Binding of Hydrophobic Ions: Application of New Kinetic Techniques.
Baumgart A, Le DT, Cranfield CG, Bridge S, Zerlotti R, Palchetti I, Tadini-Buoninsegni F, Clarke RJ.
Langmuir. 2025 Mar 18.
doi: 10.1021/acs.langmuir.4c04779. Online ahead of print.
PMID: 40102050.
Novel kinetic approach to measure the binding of hydrophobic ions to lipid bilayers.
=> reveals how binding affinity varies with ion structure and membrane composition. Experimental results support models of partitioning and local membrane perturbation.
Any1 is a phospholipid scramblase involved in endosome biogenesis.
Gao J, Franzkoch R, Rocha-Roa C, Psathaki OE, Hensel M, Vanni S, Ungermann C.
J Cell Biol. 2025 Apr 7;224(4):e202410013.
doi: 10.1083/jcb.202410013. Epub 2025 Mar 6.
PMID: 40047640.
Multivesicular bodies (MVBs) are crucial for membrane protein degradation and lipid homeostasis. Here, authors, identifie Any1 as a phospholipid scramblase that plays an important role in MVB biogenesis by coordinating membrane remodeling with lipid transfer through Vps13 at organelle contact sites.
On-the-Fly Microfluidic Control of Giant Vesicle Compositions Validated by DNA Surface Charge Sensors.
Fletcher M, Elani Y.
ACS Nano. 2025 Apr 4.
doi: 10.1021/acsnano.4c16289. Online ahead of print.
PMID: 40183490.
Microfluidic platform to dynamically control the composition of GUVs.
Surface-bound DNA sensors => real-time validation of membrane charge and lipid incorporation. This system allows precise engineering of vesicles for synthetic biology applications (e.g responsive, programmable artificial cells).
Molecules
“Living Detergents”: An In Situ Detergent Tailoring Strategy for Efficient Membrane Protein Stabilization and Analysis.
Dai Y, Yang M, Luo W, Qiu Y, Zhou F, Zheng X, Zhao F, Yao X, Zhao S, Tao H.
Chemistry. 2025 Apr 7:e202501128.
doi: 10.1002/chem.202501128. Online ahead of print.
PMID: 40192258.
“living detergents” = a dynamic strategy where detergent molecules are tailored in situ to match membrane protein requirements.
This approach improves protein stability during purification and analysis. The in situ adaptation enables compatibility with a wide range of hydrophobic surfaces and membrane protein types. This innovative method enhances the reproducibility and efficiency of structural studies.
Multiple Pendants-Bearing Triglucosides for Membrane Protein Studies: Effects of Pendant Length and Number on Micelle Interior Hydration and Protein Stability.
Sadaf A, Yun HS, Lee H, Stanfield S, Lan B, Salomon K, Woubshete M, Kim S, Ehsan M, Bae H, Byrne B, Loland CJ, Liu X, Guan L, Im W, Chae PS.
Biomacromolecules. 2025 Mar 14.
doi: 10.1021/acs.biomac.5c00036. Online ahead of print.
PMID: 40087026.
Study how the structure of detergent-like triglucosides influences the hydration and stability of MP micelles. By varying the length and number of pendant groups, the authors fine-tune micelle properties. The optimal designs improve membrane protein solubilization and stability.
The results guide rational detergent selection for membrane protein biochemistry.
Improved Pendant-Bearing Glucose-Neopentyl Glycols for Membrane Protein Stability.
Youn T, Kim G, Hariharan P, Li X, Ahmed W, Byrne B, Liu X, Guan L, Chae PS.
Bioconjug Chem. 2025 Mar 19.
doi: 10.1021/acs.bioconjchem.4c00556. Online ahead of print.
PMID: 40105011.
Newly designed glucose-neopentyl glycol detergents with pendant modifications to enhance MP stabilization. These derivatives outperform standard detergents in maintaining protein structure and function during purification. The structural flexibility of pendants allows fine-tuning of micelle characteristics.
Methods
Recent Advances in Membrane Protein Simulations.
Gumbart JC, Hanson SM.
J Phys Chem B. 2025 Mar 13;129(10):2657-2658.
doi: 10.1021/acs.jpcb.5c00803.
PMID: 40078023.
Highlight on recent progress in the simulation of MPs (methodological and computational advances).
Authors discuss how improved force fields and sampling techniques are revealing new details about protein-lipid interactions and conformational changes.
Emerging hybrid approaches, including ML integration, are also featured. The article points to the future of large-scale, accurate simulations for challenging membrane systems.
Solid-State NMR of Membrane Peptides and Proteins in the Lipid Cubic Phase.
Ramberg KO, Boland C, Kooshapur H, Soubias O, Wiktor M, Huang CY, Bailey J, Gawrisch K, Caffrey M.
Biophys J. 2025 Mar 20:S0006-3495(25)00166-3.
doi: 10.1016/j.bpj.2025.03.012. Online ahead of print.
PMID: 40119522.
solid-state NMR to investigate membrane peptides and proteins reconstituted in LCP.
Authors show that this environment provides high-resolution spectra while mimicking native membrane conditions. The technique enables analysis of protein orientation, dynamics, and interactions.
Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle.
Sampedro JG.
J Vis Exp. 2025 Mar 21;(217).
doi: 10.3791/67748.
PMID: 40193306.
Visual protocol => step-by-step purification of the SERCA pump from rabbit muscle tissue. The method yields functional enzyme suitable for biochemical and biophysical studies.
Key steps = differential centrifugation, detergent solubilization, and chromatography. souvenir souvenir …
An in vitro platform for the enzymatic characterization of the rhomboid protease RHBDL4.
Bhaduri S, Braza MKE, Stanchev S, Tauber M, Al-Bawab R, Liu LJ, Trujillo DF, Solorio-Kirpichyan K, Srivastava A, Sanlley-Hernandez J, O’Donoghue AJ, Lemberg MK, Amaro R, Strisovsky K, Neal SE.
J Biol Chem. 2025 Mar;301(3):108275.
doi: 10.1016/j.jbc.2025.108275. Epub 2025 Feb 7.
PMID: 39922490.
in vitro assay system to study the activity and substrate specificity of the rhomboid protease RHBDL4.
=> precise control over lipid environment and protease-substrate interactions. It enables kinetic and mechanistic studies relevant to membrane-associated proteolysis.
Miscelleaneous
You’re only human: a six-step strategy to surviving your PhD.
Weissbart G.
Nature. 2025 Apr 16.
doi: 10.1038/d41586-025-00967-7. Epub ahead of print.
PMID: 40240824.
For Gauthier Weissbart, psychological challenges such as uncertainty and self-doubt were more difficult to overcome than the technical or scientific issues he faced during his PhD programme in biophysics. He’s sharing six top tips for getting through a PhD “not only as a researcher, but as a human being”:
Embrace uncertainty — it fuels curiosity
Balance thinking with doing
Stop striving for perfection
Argue respectfully and listen attentively
Take breaks
Find meaning outside of work
Chew on this: The 10,000-year history of gum
Popular Science
https://www.popsci.com/science/history-of-chewing-gum/
By Lauren Leffer
Published Apr 14, 2025 8:00 AM EDT
Humans and chewing gum — or some form of it anyway — go way back. The Aztecs chewed petroleum-based natural bitumen, and before them, people in Scandinavia were chewing pitch made from the bark of birch trees. Perhaps unsurprisingly, oral hygiene was one of the main reasons people chewed back in the day. It cleaned their teeth and freshened their breath, says anthropologist Jennifer Mathews. But more than that, it likely helped people fend off hunger and thirst when resources were scarce, and could even have sharpened their senses and kept them alert.
The curious zoo of extraordinary organisms
https://bhamla.gatech.edu/
Working with artists, biomolecular engineer Saad Bhamla co-created The Curious Zoo of Extraordinary Organisms, a multilingual series of comic books that illustrate the discoveries of his lab to children. (NPR Podcast | 12 min listen)
https://www.npr.org/2025/04/14/1244690932/comic-book-bugs-superpower-cicada-pee