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
McCoy KL, Gyoneva S, Vellano CP, Smrcka AV, Traynelis SF, and 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. [Epub ahead of print].
Smrcka AV, Brown JH, and Holz GG. (2012) Role of phospholipase Cε in physiological phosphoinositide signaling networks. Cell Signal. [Epub ahead of print].
Dzhura I, Chepurny OG, Kelley GG, Leech CA, Roe MW, Dzhura E, Afshari P, Malik
S, Rindler MJ, Xu X, Lu Y, Smrcka AV, and Holz GG. (2012) Epac2-dependent mobilization of
intracellular Ca2+ by glucagon-like peptide-1 receptor agonist exendin-4 is
disrupted in beta-cells of phospholipase C-epsilon knockout mice. J Physiol. [Epub ahead of print].
Lin Y, and Smrcka AV. (2011) Understanding molecular recognition by G protein βγ subunits on the path to pharmacological targeting. Mol. Pharmacol. 80:551-557.
Seneviratne AM, Burroughs M, Giralt E, and Smrcka AV. (2011) Direct-reversible binding of small molecules to G protein βγ subunits. Biochim. Biophys. Acta 1814:1210-1218.
Zhang L, Malik S, Kelley GG, Kapiloff MS, and Smrcka AV. (2011) Phospholipase C{epsilon} scaffolds to muscle-specific A kinase anchoring protein (mAKAP{beta}) and integrates multiple hypertrophic stimuli in cardiac myocytes. J. Biol. Chem. 286:23012-2321.
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 |
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Lianghui Zhang Graduate Student, Pharmacology and Physiology Ph.D. Program |
