2024/01/10 by Yi‐Hsuan Lin, Yi-Hsuan Lin, Tae Hun Kim +10 · 27 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · Engineering · Materials Science · #Biology #Biophysics #Chemical physics #Chemistry #Condensed matter physics #Electrical engineering #Electrostatics #Engineering #Enzyme Structure and Function #Materials science #Nanotechnology #Phase (matter) #Physics #Protein Structure and Dynamics #RNA Research and Splicing #Reentrancy #Salt (chemistry) #Static electricity
paper · pdf · open access · doi:10.7554/elife.100284
published in eLife 13 (eLife Sciences Publications Ltd)
openalex publication_date 2024/09/05 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/05
Liquid-liquid phase separation (LLPS) involving intrinsically disordered protein regions (IDRs) is a major physical mechanism for biological membraneless compartmentalization. The multifaceted electrostatic effects in these biomolecular condensates are exemplified here by experimental and theoretical investigations of the different salt- and ATP-dependent LLPSs of an IDR of messenger RNA-regulating protein Caprin1 and its phosphorylated variant pY-Caprin1, exhibiting, for example, reentrant behaviors in some instances but not others. Experimental data are rationalized by physical modeling using analytical theory, molecular dynamics, and polymer field-theoretic simulations, indicating that interchain ion bridges enhance LLPS of polyelectrolytes such as Caprin1 and the high valency of ATP-magnesium is a significant factor for its colocalization with the condensed phases, as similar trends are observed for other IDRs. The electrostatic nature of these features complements ATP's involvement in π-related interactions and as an amphiphilic hydrotrope, underscoring a general role of biomolecular condensates in modulating ion concentrations and its functional ramifications.