Pablo Rivera Fuentes

Biographie

Pablo Rivera-Fuentes was born in 1984 in Mexico City. He received a BSc (2008) degree in chemical engineering from the National Autonomous University of Mexico. He obtained his MSc (2009) and PhD (2012) degrees in chemistry from ETH Zurich, working under the supervision of Prof. François Diederich. His dissertation was awarded the ETH Medal in 2013. Funded by the Swiss National Science Foundation (SNSF), he carried out postdoctoral research at Massachusetts Institute of Technology with Prof. Stephen J. Lippard (2012-2014). He subsequently worked at the University of Oxford with Prof. Harry L. Anderson (Department of Chemistry) and Prof. Christian Eggeling (Weatherall Institute of Molecular Medicine). He started his independent career as non-tenure-track assistant professor at ETH Zurich in October, 2015, and became tenure-track assistant professor of chemical biology at EPFL in August, 2019.

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https://people.epfl.ch/pablo.riverafuentes?lang=fr

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Publications associées (51)

A locally activatable sensor for robust quantification of organellar glutathione

Gianluca Quargnali, Pablo Rivera Fuentes

Glutathione (GSH) is the main determinant of intracellular redox potential and participates in multiple cellular signalling pathways. Achieving a detailed understanding of intracellular GSH homeostasis depends on the development of tools to map GSH compartmentalization and intra-organelle fluctuations. Here we present a GSH-sensing platform for live-cell imaging, termed targetable ratiometric quantitative GSH (TRaQ-G). This chemogenetic sensor possesses a unique reactivity turn-on mechanism, ensuring that the small molecule is only sensitive to GSH in a desired location. Furthermore, TRaQ-G can be fused to a fluorescent protein to give a ratiometric response. Using TRaQ-G fused to a redox-insensitive fluorescent protein, we demonstrate that the nuclear and cytosolic GSH pools are independently regulated during cell proliferation. This sensor was used in combination with a redox-sensitive fluorescent protein to quantify redox potential and GSH concentration simultaneously in the endoplasmic reticulum. Finally, by exchanging the fluorescent protein, we created a near-infrared, targetable and quantitative GSH sensor.

NATURE PORTFOLIO2023

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Single-Molecule Peptide Identification Using Fluorescence Blinking Fingerprints

Salome Riccarda Püntener, Pablo Rivera Fuentes

The ability to identify peptides with single-molecule sensitivity would lead to next-generation proteomics methods for basic research and clinical applications. Existing single-molecule peptide sequencing methods can read some amino acid sequences, but they are limited in their ability to distinguish between similar amino acids or post-translational modifications. Here, we demonstrate that the fluorescence intermittency of a peptide labeled with a spontaneously blinking fluorophore contains information about the structure of the peptide. Using a deep learning algorithm, this single-molecule blinking pattern can be used to identify the peptide. This method can distinguish between peptides with different sequences, peptides with the same sequence but different phosphorylation patterns, and even peptides that differ only by the presence of epimerized residues. This study builds the foundation for a targeted proteomics method with single-molecule sensitivity.

AMER CHEMICAL SOC2023

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Single-molecule localization microscopy (SMLM) can reveal nanometric details of biological samples, but its high phototoxicity hampers long-term imaging in live specimens. A significant part of this phototoxicity stems from repeated irradiations that are necessary for controlled switching of fluorophores to maintain the sparse labeling of the sample. Lower phototoxicity can be obtained using fluorophores that blink spontaneously, but controlling the density of single-molecule emitters is challenging. We recently developed photoregulated fluxional fluorophores (PFFs) that combine the benefits of spontaneously blinking dyes with photocontrol of emitter density. These dyes, however, were limited to imaging acidic organelles in live cells. Herein, we report a systematic study of PFFs that culminates in probes that are functional at physiological pH and operate at longer wavelengths than their predecessors. Moreover, these probes are compatible with HaloTag labeling, thus enabling timelapse, single-molecule imaging of specific protein targets for exceptionally long times.

WILEY-V C H VERLAG GMBH2022

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