La Noche Europea de los Investigadores e Investigadoras es una oportunidad perfecta para poner en valor la #ciencia, con más de 100 actividades y la participación de 358 investigadores en Aragón. Para la @unizar.es es un orgullo organizar esta jornada, con talleres, paseos y monólogos científicos.

Extraordinaria noche europea (y día) de los investigadores e investigadoras en Zaragoza! Dos días hablando del trabajo que hacemos en el instituto BIFI. Hemos acabado sin voz pero muy muy orgullosos de la ciencia aragonesa! Exitazo! @ucc.unizar.es, @unizar.es, @lma-unizar.bsky.social

And last but not least, thanks to all the cryo-EM facilities (and their local contacts), where we optimized grids and collected cryo-EM data: @necen.bsky.social, @esrf.fr, BREM, CNIO, CIB and @lma-unizar.bsky.social and SAI @unizar.es

Many thanks to Carlos Vega-Gutiérrez, Irene Sánchez and Victoria Ribón from my lab at BIFI in @unizar.es, and Javier Picañol and David Soto from @ub.edu; thanks to all the funding agencies, @ageinves.bsky.social, FSE, and DGA,

While GluA4 shares the Y-shaped architecture of GluA2, during desensitization its LBD dimers rupture, resembling GluA1 and GluA3 complexes. This rupture is observed even under resting conditions. We also identified a new site for TARP modulation, located near the flip/flop region

Extremely happy to share our lab’s first paper now published in @NatureSMB! We determined the cryo-EM structures of GluA4, both alone and in complex with TARP2, capturing the receptor in different functional states.

GluA4 AMPA receptor gating mechanisms and modulation by auxiliary proteins Nature Structural & Molecular Biology, Published online: 15 September 2025; doi:10.1038/s41594-025-01666-7Vega-Gutiérrez et al. present cryo-electron microscopy structures of GluA4-containing AMPA receptors, which are key for brain signaling. They show GluA4-specific conformations and explain how subunit composition shapes receptor architecture, dynamics and function.

New online: GluA4 AMPA receptor gating mechanisms and modulation by auxiliary proteins

Cryo-EM maps of GluA2/TARP-γ2 (red) and GluA3/TARP-γ2 (green)

New research from @igreger.bsky.social group in the LMB’s Neurobiology Division, show that GluA3 adopts a structural organization that substantially diverges from all the other AMPA receptors.

Read more: www2.mrc-lmb.cam.ac.uk/architecture...

#LMBResearch

Happy about our new paper in Nature rdcu.be/eukUB
The GluA3 structure provides a framework for understanding this disease-prone glutamate receptor - novel interfaces will provide targets for modulator development

Desde el equipo de gobierno y dado que se ha restablecido el suministro eléctrico, se recupera con normalidad la actividad laboral y académica a partir de mañana, 29 de abril en el horario habitual.

Queremos agradecer a toda la comunidad universitaria su colaboración, comprensión y paciencia.