When:
Monday, May 1, 2017
4:00 PM - 5:00 PM CT
Where: Ward Building, 5-230, 303 E. Chicago Avenue, Chicago, IL 60611 map it
Audience: Faculty/Staff - Student - Public - Post Docs/Docs - Graduate Students
Contact:
Alexa Nash
(312) 503-4893
Group: Department of Pharmacology Seminars
Category: Lectures & Meetings
The Department of Pharmacology is pleased to welcome Dr. Yubin Zhou, Ph.D., Associate Professor & ACS Research Scholar, Department of Medical Physiology, Texas A&M University
The following, is an overview of this seminar, as described by Dr.Zhou:
The application of current channelrhodopsin-based optogenetic tools is limited by the lack of strict ion selectivity and the inability to extend the spectra sensitivity into the near-infrared (NIR) tissue transmissible range. Here we present an NIR-stimulable optogenetic platform based on the stromal interaction molecule 1 (STIM1) that selectively and remotely controls Ca2+ oscillations and Ca2+-dependent activities in mammalian cells. When coupled to upconversion nanoparticles, the optogenetic operation window is shifted from the visible range to NIR wavelengths to enable wireless and remote photoactivation of Ca2+-dependent signaling and optogenetic modulation of immunoinflammatory responses. In a mouse model of melanoma by using ovalbumin as surrogate tumor antigen, Opto-CRAC has been shown to act as a genetically-encoded “photoactivatable adjuvant” to improve antigen-specific immune responses to specifically destruct tumor cells. In addition, we have extended optogenetic engineering approaches to photomanipulate membrane contact sites that play critical roles in controlling lipid metabolism and calcium signaling. We created a set of novel tools to reversibly control the formation of membrane contact sites at high spatiotemporal resolution. This optogenetic tool opens new opportunities for i) dynamically examining lipid-protein interaction by a simple grafting approach; ii) delivering proteins of interest to this specialized subcellular compartment; and iii) screening protein and chemical modulators that are involved in maintaining and remodeling ER-PM junctions. Our study represents a solid step forward towards the goal of achieving remote control of Ca2+-modulated activities at membrane contact sites with tailored function. Finally, we will report our recent progress in developing novel optogenetic platforms that can be used as modular scaffolds to control protein function with light.