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Distinct liquid-liquid phase separation properties of end-binding proteins EB1 and EB3.

Solomiia Boyko1, Qiuye Li1, Krystyna Surewicz1

  • 1Department of Physiology and Biophysics, Case Western Reserve University, Cleveland, Ohio, USA.

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End-binding proteins (EBs) form condensates that regulate microtubule dynamics. EB3 proteins exhibit greater liquid-liquid phase separation (LLPS) propensity than EB1, influencing tubulin polymerization differently.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Molecular Dynamics

Background:

  • End-binding proteins (EBs) are key microtubule-plus-end-tracking proteins (+TIPs).
  • EBs are known to undergo liquid-liquid phase separation (LLPS), forming condensates.
  • These condensates are proposed to recruit other +TIPs and influence tubulin polymerization.

Purpose of the Study:

  • To investigate the LLPS properties of EB1 and EB3 in mammalian cells.
  • To compare the LLPS propensity and condensate material properties of EB1 and EB3.
  • To determine how EB1 and EB3 condensates affect tubulin polymerization, individually and with CLIP-170.

Main Methods:

  • In vitro and in-cell studies of EB1 and EB3.
  • Analysis of protein sequence identity and domain contributions to LLPS.
  • Characterization of condensate material properties (dynamics).
  • Assessment of tubulin recruitment and polymerization nucleation by EB condensates.

Main Results:

  • EB3 shows significantly higher LLPS propensity than EB1, attributed to multiple regions including N-terminal histidines.
  • EB3 condensates are less dynamic than EB1 condensates.
  • EB3 droplets exhibit a greater capacity for tubulin recruitment and polymerization nucleation.
  • Differences in EB1/EB3 condensate properties are amplified in the presence of CLIP-170, impacting tubulin polymerization.

Conclusions:

  • Distinct EB1 and EB3 condensates possess different material properties.
  • These differences lead to functional specialization in microtubule dynamics and tubulin polymerization.
  • The findings suggest the existence of distinct EB-dependent +TIP bodies in cells.