Publicaciones de Pablo Galaz-Davison
2026
Peña-Vilches, Nicolás; González-Avendaño, Mariela; Soto-García, Nicole; Maureira, Diego; Silva, Ian; Avilés, Javiera; Manríquez-Benítez, Elías; Medina, Exequiel; Cerda, Oscar; Galaz-Davison, Pablo; Vergara-Jaque, Ariela
Identification of 14-3-3 Proteins as Binding Partners of TRP Channels Artículo de revista
En: 2026.
@article{Peña-Vilches2026,
title = {Identification of 14-3-3 Proteins as Binding Partners of TRP Channels},
author = {Nicolás Peña-Vilches and Mariela González-Avendaño and Nicole Soto-García and Diego Maureira and Ian Silva and Javiera Avilés and Elías Manríquez-Benítez and Exequiel Medina and Oscar Cerda and Pablo Galaz-Davison and Ariela Vergara-Jaque},
doi = {10.1021/acs.jcim.6c00092},
year = {2026},
date = {2026-03-16},
abstract = {Transient receptor potential (TRP) channels are regulated by a diverse network of intracellular partners that govern their trafficking, stability, and functional expression at the plasma membrane. Here, we present a comprehensive and integrative characterization of 14-3-3 proteins as conserved binding partners of TRP channels. Leveraging the extensive structural repertoire of 14-3-3 complexes resolved to date, we combined large-scale sequence and structural analyses with molecular docking, coevolutionary inference, machine learning-based predictions, atomistic simulations, and targeted experimental validation to elucidate the molecular principles underlying TRP-14-3-3 recognition. Integration of these approaches into a unified consensus scoring framework revealed recurrent, solvent-exposed cytoplasmic motifs across the TRP channel family with a high propensity for 14-3-3 binding. Focusing on the TRPM4-14-3-3γ interaction, we identified an N-terminal cytoplasmic region of the channel as the primary 14-3-3 binding hotspot. Structural modeling and molecular dynamics simulations revealed a stable electrostatically driven interface, which was experimentally validated by fluorescence anisotropy assays. Moreover, biochemical and functional analyses demonstrated that TRPM4 interacts not only with 14-3-3γ but also with 14-3-3η, leading to a reduced channel-mediated sodium influx. Together, these findings establish 14-3-3 proteins as general and evolutionarily conserved regulators of TRP channels and provide a broadly applicable framework for identifying transient protein–protein interactions relevant to TRP channel dysregulation in disease.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Transient receptor potential (TRP) channels are regulated by a diverse network of intracellular partners that govern their trafficking, stability, and functional expression at the plasma membrane. Here, we present a comprehensive and integrative characterization of 14-3-3 proteins as conserved binding partners of TRP channels. Leveraging the extensive structural repertoire of 14-3-3 complexes resolved to date, we combined large-scale sequence and structural analyses with molecular docking, coevolutionary inference, machine learning-based predictions, atomistic simulations, and targeted experimental validation to elucidate the molecular principles underlying TRP-14-3-3 recognition. Integration of these approaches into a unified consensus scoring framework revealed recurrent, solvent-exposed cytoplasmic motifs across the TRP channel family with a high propensity for 14-3-3 binding. Focusing on the TRPM4-14-3-3γ interaction, we identified an N-terminal cytoplasmic region of the channel as the primary 14-3-3 binding hotspot. Structural modeling and molecular dynamics simulations revealed a stable electrostatically driven interface, which was experimentally validated by fluorescence anisotropy assays. Moreover, biochemical and functional analyses demonstrated that TRPM4 interacts not only with 14-3-3γ but also with 14-3-3η, leading to a reduced channel-mediated sodium influx. Together, these findings establish 14-3-3 proteins as general and evolutionarily conserved regulators of TRP channels and provide a broadly applicable framework for identifying transient protein–protein interactions relevant to TRP channel dysregulation in disease.
2025
Galaz-Araya, Constanza; Galaz-Davison, Pablo; Cortés-Arriagada, Diego; Zamora, Ricardo A.; Poblete, Horacio
Molecular Dynamics Study on the Influence of the CLK Motif on the Structural Stability of Collagen-Like Peptides Adsorbed on Gold Nanosurfaces Artículo de revista
En: ACS Omega, vol. 10, no 10, pp. 10366–10374, 2025, ISSN: 2470-1343.
@article{Galaz-Araya2025,
title = {Molecular Dynamics Study on the Influence of the CLK Motif on the Structural Stability of Collagen-Like Peptides Adsorbed on Gold Nanosurfaces},
author = {Constanza Galaz-Araya and Pablo Galaz-Davison and Diego Cortés-Arriagada and Ricardo A. Zamora and Horacio Poblete},
doi = {10.1021/acsomega.4c10450},
issn = {2470-1343},
year = {2025},
date = {2025-03-18},
journal = {ACS Omega},
volume = {10},
number = {10},
pages = {10366--10374},
publisher = {American Chemical Society (ACS)},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
