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Updated: Jun 25, 2026

Chemical Dimerization-Induced Protein Condensates on Telomeres
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Published on: April 12, 2021

Dissecting the propensity of RIM1 subdomains to form phase condensates.

Luis Kersten1, Maksim Galkov1, Paulina Nemcova1

  • 1Institute of Cellular Neurosciences II, University Hospital Bonn, University of Bonn, Venusberg Campus 1, 53127, Bonn, Germany.

Scientific Reports
|June 23, 2026
PubMed
Summary

Liquid-liquid phase separation (LLPS) drives synaptic protein organization. Researchers found that even short fragments of the active zone protein RIM1 can form biomolecular condensates, with longer fragments showing increased enrichment.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Liquid-liquid phase separation (LLPS) is increasingly recognized for its role in organizing synaptic vesicle and active zone (AZ) proteins within presynaptic terminals.
  • Understanding the intrinsic factors governing a protein's LLPS propensity, such as structural disorder and post-translational modifications, is crucial for dissecting condensate formation in a cellular context.

Purpose of the Study:

  • To systematically investigate the condensation properties of the active zone protein RIM1 and its fragments within a cellular environment.
  • To identify the minimal sequence elements responsible for RIM1's phase separation behavior and condensate formation.

Main Methods:

  • Utilized a cell-based overexpression assay in HEK cells to examine the condensation propensity of full-length RIM1 and various RIM1 fragments.
  • Quantitatively correlated fragment length with enrichment in condensate-like assemblies.
  • Assessed the impact of RIM-BP2 on RIM1 phase condensation at different expression levels.

Main Results:

  • Full-length RIM1 demonstrated the highest condensation propensity, but fragments as short as ~250 amino acids formed condensate-like assemblies.
  • The propensity for fragment enrichment in droplets generally increased with fragment length.
  • A minimal region, including zinc finger, IDR1, PRM1, PDZ, and C2A domains, was identified that replicated key condensate properties of full-length RIM1.
  • RIM-BP2 modulated RIM1 condensation, with effects varying based on RIM1 expression levels and truncation status.

Conclusions:

  • Defined the phase condensation behavior of distinct RIM1 sequence elements.
  • Demonstrated that the enrichment of RIM1 within phase condensates exhibits an exponential increase with fragment length.
  • Provided insights into the structural determinants of RIM1's ability to form biomolecular condensates, relevant to synaptic organization.