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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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The mitochondrial cristae membrane is the primary site for the oxidative phosphorylation (OXPHOS) process of energy conversion mediated through respiratory complexes I to V. These complexes have been widely studied for decades, and it has been proven that they form supramolecular structures called respiratory supercomplexes (SC). These higher-order complexes may be crucial in maintaining the biochemical structure and improving the physiological activity of the individual complexes while...
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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Updated: Feb 24, 2026

Reconstitution of Septin Assembly at Membranes to Study Biophysical Properties and Functions
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Formación de supercomplejos inducida por proteínas y tensión de membrana

Maximilian C Pöverlein1, Alexander Jussupow1, Hyunho Kim1

  • 1Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.

eLife
|February 23, 2026
PubMed
Resumen

Los supercomplejos de la cadena de transporte de electrones en las mitocondrias reducen la tensión de la membrana, mejorando la producción de ATP. Este ensamblaje optimiza la función respiratoria en entornos celulares abarrotados.

Palabras clave:
bioenergéticabiofísica moleculardinámica molecularinteracciones proteína-membranacomplejos respiratoriosbiología estructuralsupercomplejos

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Área de la Ciencia:

  • Biología mitocondrial
  • Biofísica
  • Dinámica molecular

Sus antecedentes:

  • Las membranas mitocondriales contienen la cadena de transporte de electrones (ETC) esencial para la síntesis de ATP a través de la fosforilación oxidativa (OXPHOS).
  • Las proteínas de la ETC se ensamblan en supercomplejos (SC), pero su significado funcional es objeto de debate.

Objetivo del estudio:

  • Investigar el papel funcional de los supercomplejos de la ETC de mamíferos, específicamente el SC I/III2.
  • Comprender cómo la formación de SC impacta las propiedades de la membrana mitocondrial y la dinámica de las proteínas.

Principales métodos:

  • Simulaciones moleculares atomísticas y de grano grueso a gran escala.
  • Análisis de datos de microscopía electrónica criogénica.
  • Modelado estadístico y cinético.

Principales resultados:

  • La formación de SC I/III2 de mamíferos alivia la tensión de la membrana mitocondrial interna al modificar el grosor local de la membrana.
  • El ensamblaje de SC promueve la acumulación de cardiolipina y quinonas alrededor del supercomplejo.
  • La formación de supercomplejos influye en el movimiento global de las proteínas individuales de la ETC.

Conclusiones:

  • La aglomeración molecular y la tensión de la membrana actúan como impulsores termodinámicos para la formación de SC.
  • El ensamblaje de SC puede mejorar el flujo respiratorio en membranas abarrotadas bajo condiciones restringidas.