Smrcka Lab
Alan V. Smrcka, Ph.D.
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Affiliations:
- Cellular and Molecular Pharmacology and Physiology
- Biochemistry and Molecular Biology
- Biophysics, Structural and Computational Biology
Research Overview
We work with the tools of biology, chemistry, and genetics to understand basic mechanisms of cellular signaling and develop therapeutic strategies for heart disease, cancer, and inflammatory diseases.
G protein coupled receptors (GPCRs) form a large family of cell surface receptors responsible for triggering cellular responses to a large number of extracellular stimuli including hormones such as adrenaline, serotonin, or acetylcholine and receive sensory stimuli responsible for perception of light, smell, and taste. This family of receptors is an important target for pharmaceuticals and defects in GPCR systems and are responsible for a number of diseases. All GPCRs function through activation of trimeric G proteins located on the inner surface of the plasma membrane. When GPCRs interact with an activating ligand they bind to the G protein and catalyze their activation. The activated G proteins then target ion channels or enzymes that produce second messengers to regulate cell physiology and growth.
We use chemical, structural and genetic methods to understand and manipulate G protein pathways. Because of the underlying involvement of G protein signaling in many aspects of cellular physiology, targeting these pathways has many implications for therapy.
Projects
G Proteins |
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Phospholipases |
Recent Publications
Dusaban SS, Purcell NH, Rockenstein E, Masliah E, Cho MK, Smrcka AV, Brown JH. (2013) Phospholipase C{varepsilon} links G protein-coupled receptor activation to inflammatory astrocytic responses. Proc Natl Acad Sci U S A. [Epub ahead of print]
Dbouk HA, Vadas O, Shymanets A, Burke JE, Salamon RS, Khalil BD, Barrett MO, Waldo GL, Surve C, Hsueh C, Perisic O, Harteneck C, Shepherd PR, Harden TK, Smrcka AV, Taussig R, Bresnick AR, Nürnberg B, Williams RL, Backer JM. (2012) G protein-coupled receptor-mediated activation of p110β by Gβγ is required for cellular transformation and invasiveness. Sci Signal. 5(253):ra89.
McCoy KL, Gyoneva S, Vellano CP, Smrcka AV, Traynelis SF, Hepler JR. (2012) Protease-activated receptor 1 (PAR1) coupling to G(q/11) but not to G(i/o) or G(12/13) is mediated by discrete amino acids within the receptor second intracellular loop. Cell Signal. 24:1351-1360.
Smrcka AV, Brown JH, Holz GG. (2012) Role of phospholipase Cε in physiological phosphoinositide signaling networks. Cell Signal. 24:1333-1343.
Contact Us
Alan V. Smrcka, Ph.D.
University of Rochester
School of Medicine and Dentistry
Box 711
601 Elmwood Avenue
Rochester, NY 14642
Telephone: 585-275-0892
Fax: 585-273-2652
Alan_Smrcka@
urmc.rochester.edu
Lab Members |
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Michael B. Burroughs Technical Staff |
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Wei Kan Graduate Student, Pharmacology and Physiology Ph.D. Program |
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Sundeep Malik Research Faculty |
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Nancy C. Ward Technical Staff |
