SpruijtLab

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  SpruijtLab spruijtlab.bsky.social · Jul 16, 2025
  New in JACS! Using NMR, we show how condensates selectively bind and localize ions following the 'law of matching water affinities', shaping condensate composition, interface potential & RNA stability. Read about it here: doi.org/10.1021/jacs.5c07295 @irissmokers.bsky.social
  

  Selective Ion Binding and Uptake Shape the Microenvironment of Biomolecular Condensates

  Biomolecular condensates modulate various ion-dependent cellular processes and can regulate subcellular ion distributions by selective uptake of ions. To understand these processes, it is essential to...

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  Mesoscopic Physics of Life (MPoL) m-pol.bsky.social · Jun 26, 2025
  Excited to share our new JACS paper "Controlling Multiphase Coacervate Wetting and Self‑Organization by Interfacial Proteins" Together with our fantastic collaborators @spruijtlab.bsky.social l we show how surface-active proteins tune condensate architecture and organization.
  

  Controlling Multiphase Coacervate Wetting and Self-Organization by Interfacial Proteins

  Biomolecular condensates help organize biochemical processes in cells and synthetic cell analogues. Many condensates exhibit multiphase architectures, yielding compartments with distinct functions. Ho...

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  SpruijtLab spruijtlab.bsky.social · Jun 18, 2025
  We’re pleased to announce that our JACS paper with our collaborators @m-pol.bsky.social 'Controlling Multiphase Coacervate Wetting and Self‑Organization by Interfacial Proteins' is now online! Read here: doi.org/10.1021/jacs...
  

  Controlling Multiphase Coacervate Wetting and Self-Organization by Interfacial Proteins

  Biomolecular condensates help organize biochemical processes in cells and synthetic cell analogues. Many condensates exhibit multiphase architectures, yielding compartments with distinct functions. However, how cells regulate the transformation between different multiphase architectures remains poorly understood. Here, we use multiphase coacervates as model condensates and present a new approach to control wetting and self-organization in multiphase coacervates by introducing a surface-active protein, α-synuclein (αSyn). αSyn can localize at the interface of uridine 5′-triphosphate (UTP)/poly-l-lysine (pLL)/oligo-l-arginine (R10) multiphase coacervates and induce the transformation from nested droplets into partially wetted droplets. The exposed UTP/R10 core coacervate droplets adhered to neighboring (shell) coacervates, forming structures similar to polymers and leading to a dynamic yet stable self-organized network of connected coacervates, which we call coacervate polymers. A theoretical model demonstrates that multiphase coacervates transition to partial wetting upon increasing the interfacial protein, consistent with experimental observations. When three neighboring coacervates are not aligned, surface tension straightens their arrangement, similar to semiflexible polymers. This mechanism likely extends to larger structures, promoting chain formation while preventing fusion. Interestingly, diverse proteins were found to be surface active in multiphase coacervates: BSA, mCherry, and FtsZ all exhibited the same effect on multiphase coacervates’ partial wetting and organization. These findings suggest that interfacial proteins could be used by cells not only to stabilize condensates, but also to control multiphase organization and to regulate the interaction between condensates.

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  SpruijtLab spruijtlab.bsky.social · Jan 28, 2025
  Some great work on the role of PMLII condensates in nuclear envelope repair by Anne, now on bioRxiv! Read here: www.biorxiv.org/content/10.1...
  

  Patching up the nucleus: a novel role for PMLII in nuclear envelope rupture repair

  The nuclear envelope (NE) is important for cellular health as it protects and organizes the genome. NE dynamics is important for various cellular processes including cell growth, migration and removal...

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  bioRxiv Cell Biology handle.invalid · Jan 24, 2025
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