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The first TRP channel was identified in 1977 as a phototransduction mutant in Drosophila (Minke, 1977). Since that time the TRP channel family has grown to include at least 20 members (Clapham et al., 2001). The importance of TRP channels is demonstrated by the wide variety of their proposed functions: invertebrate phototransduction; responding to painful stimuli; responding to moderate temperature changes; repletion of intracellular calcium stores; receptor–mediated excitation; and modulation of the cell cycle (reviewed in (Clapham et al., 2001; Montell, 2001; Montell et al., 2002). Despite the clear physiological importance of TRP channels, little is known about what regulates their function. One type of TRP channel, TRPV1, is a polymodal receptor that integrates a number of painful stimuli. These stimuli include: noxious heat, with a threshold of approximately 42°C; extracellular acidification, with a pKa of about 5.3 (Caterina et al., 1997; Jordt et al., 2000); anandamide and other arachidonic acid metabolites (Smart et al., 2000); and capsaicin, a pungent extract from plants in the Capsicum family (Szallasi and Blumberg, 1999; Caterina and Julius, 2001).

Our lab lab studies the molecular mechanisms of activation and regulation of TRPV1 channels. We use electrophysiology to study their functional properties, molecular biology to control their primary sequence (i.e. make mutations), and biochemistry to examine their interactions with other proteins. We are particularly interested in interactions. For ion channels, we must consider interactions between subunits within one channel, interactions with regulator proteins, interactions with the membrane, and interactions with small molecules such as second messengers. It is through understanding what interactions occur, when they occur, and how they have their effect that we make progress in addressing the function and role of ion channels within cells.


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Sharona Gordon, Professor seg [at] uw.edu

Mika Munari, Research Scientist mawaya [at] uw.edu

Eric Senning, Postdoctoral Fellow endsen [at] uw.edu

I use fluorescence microscopy and Ca2+ sensitive dyes to record the time-dependent behavior of single TRPV1 ion channels opening and closing in the cell. My studies revealed that TRPV1 became slower with time that it remained open (Senning et al., eLife 2015). In the figure to the left I observe Ca2+ sparklets overlap with mobile TRPV1-GFP in plasma membrane of a HEK293T /17 cell. (A) Track of TRPV1-GFP with sparklet image as background. Clicking on image provides further examples of sparklets. (B) Fluorescence intensity of mobile TRPV1-GFP in (A). Sustained higher intensities correspond to sparklet activity. Arrowhead indicates acquisition of image in (A).

Cell unroofing is the process by which we remove the body of an adherent cell grown on a coverslip so that the only remaining cellular material on the coverslip is a plasma membrane sheet. Our recent structural studies of TRPV1 with an unnatural amino acid (UAA) inserted at different sites along its polypeptide sequence relied on sonication as the unroofing method (Zagotta et al., JGP 2016). To the left are examples of unroofed HEK293T/17 cells. (A) A plasma membrane sheet loaded with fluorescent Rhodamine B C-18. Brighter regions on periphery indicate partial unroofing where two bilayers are still present. Clicking on this image shows an unroofing movie of a cell expressing the PIP2 marker PLCδ-PH-GFP. The fluorescence intensity decreases after unroofing as the PLCδ-PH-GFP dissociates from the membrane. (B) A cell (outline in white) expressing TRPV1-GFP has a region of diffuse background fluorescence (yellow dashed line). The plasma membrane with resident TRPV1-GFP single channels remains after unroofing while intracellular TRPV1-GFP (presumably in endoplasmic reticulum and other intracellular membranes) is lost. See movie: TRPV1-GFP_unroof.m4v.

Gilbert Martinez, Postdoctoral Fellow gman [at] uw.edu

Click Here for Gilbert's Website

I’m interested in membrane protein structure-function with an emphasis on the 6-TM voltage gated ion channel superfamily. I use a broad array of biochemical and biophysical techniques to study the energetics of channel activation/inactivation/closing and how channel environment (cell-type, lipid composition, etc.) influence the energetics.


Mario Rosasco, Postdoctoral Fellow mrosasco [at] uw.edu

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Mario received his BA in biology from the University of Chicago in 2009, where he specialized in neuroscience and endocrinology. He was awarded his Ph.D. from the department of Pharmacology at the University of Washington in 2014, and has been a postdoc in the Gordon lab since 2015.


Anastasiia Stratiievska, Graduate Student nastyna [at] uw.edu

A graduate student in Department of Physiology and Biophysics PhD program since 2015. Transferred from graduate program at Bogomoletz Institute of Physiology, International Center for Molecular Physiology, Kyiv, Ukraine since 2012. In 2012 she obtained her Master’s Degree in Molecular Physiology and Biophysics from Moscow Institute of Physics and Technology (State University, Kyiv affiliate), Dept. of Molecular and Biological Physics, Kyiv, Ukraine.

Undergraduate Research Assistants

Nicolas Basil
Sarah Nelson
Amanda Qu
Nicolas Reyes

Sharona Gordon
University of Washington
HSB Room I-312

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