Structure, Function and Modulation of Ion Channels

Our Lab

Dissecting ion channels with biophysical and chemical approaches


Our laboratory investigates the glycosylation, assembly, structure, trafficking and function of ion channel complexes. We rely on traditional electrophysiological, biochemical, and imaging modalities, but we also design, develop, and utilize novel chemical tools to interrogate a wide variety of ion channels and membrane transport proteins responsible for cardiac and neuronal function. Thus, we have synthetic organic chemists, glycobiologists, membrane protein biochemists, and electrophysiologists working together to elucidate the molecular underpinnings of these membrane transport proteins in both healthy and diseased tissues.

Meet the Lab


Research Focus

Exploiting the cell's glycocalyx to visualize extracellular fluxes

Given the laboratory's enthusiasm for studying ion channels, our lab has been developing a new approach to visualize ions exiting and entering cells. Our first publication in Cell Chemical Biology enabled the visualization of proton accumulation and depletion on the extracellular side of the membrane. Proton fluxes were visualized from voltage-gated ion channels, transporters, and mutant channels harboring mutations associated with human disease. The video (left) shows protons rushing into a cell after the channels were opened with hyperpolarizing pulse (-120 mV). The initial fluorescent signal is due to protonated fluorescent sensors covalently attached to the cell's glycocalyx. Proton channel activation at -120 mV results in proton depletion and loss of the fluorescent signal, which slowly returns after the channels are closed (30 mV).

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  • The Proton-Coupled Monocarboxylate Transporter Hermes Is Necessary for Autophagy during Cell Death.

    Related Articles

    The Proton-Coupled Monocarboxylate Transporter Hermes Is Necessary for Autophagy during Cell Death.

    Dev Cell. 2018 Oct 09;:

    Authors: Velentzas PD, Zhang L, Das G, Chang TK, Nelson C, Kobertz WR, Baehrecke EH

    Nutrient availability influences the production and degradation of materials that are required for cell growth and survival. Autophagy is a nutrient-regulated process that is used to degrade cytoplasmic materials and has been associated with human diseases. Solute transporters influence nutrient availability and sensing, yet we know little about how transporters influence autophagy. Here, we screen for solute transporters that are required for autophagy-dependent cell death and identify CG11665/hermes. We show that hermes is required for both autophagy during steroid-triggered salivary gland cell death and TNF-induced non-apoptotic eye cell death. hermes encodes a proton-coupled monocarboxylate transporter that preferentially transports pyruvate over lactate. mTOR signaling is elevated in hermes mutant cells, and decreased mTOR function suppresses the hermes salivary gland cell death phenotype. Hermes is most similar to human SLC16A11, a protein that was recently implicated in type 2 diabetes, thus providing a link between pyruvate, mTOR, autophagy, and possibly metabolic disorders.

    PMID: 30318245 [PubMed - as supplied by publisher]

All Publications


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Contact Us

Lazare Research Building 804
Campus Map (pdf)

508.856.8861 (office)
508.856.6722 (lab)


Mailing Address:
William R. Kobertz, Ph.D.
Department of Biochemistry and Molecular Pharmacology
University of Massachusetts Medical School
364 Plantation Street LRB804, Worcester, MA 01605-4321

Join Us

We are always interested in applications from qualified candidates at the postdoctoral and research associate levels. UMMS GSBS graduate students interested in rotating in the Kobertz Lab should email Dr. Kobertz to set up an appointment.

Undergraduates interested in pursuing a PhD at UMass Medical School should apply directly to the Graduate School of Biomedical Sciences Program.