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Email

saraw@bcm.edu

Positions

Postdoctoral Associate - Mentor: Ted Wensel, Ph.D.

Biochemistry-Wensel Lab
²ÝÁñÉçÇøÈë¿Ú
Houston, TX US

Addresses

²ÝÁñÉçÇøÈë¿Ú (Lab)

BCM-Cullen Building
Room: BCMC-N430
Houston, TX 77030
United States

Education

PhD from University of California

08/2010 - Riverside, California United States

Biochemistry and Molecular Biology

BS from California State Polytechnic University

06/2003 - Pomona, California United States

Chemistry

Honors & Awards

IRACDA (Institutional Research and Academic Career Development Award) postdoctoral Fellow

Teaching and Research Postdoctoral Program

²ÝÁñÉçÇøÈë¿Ú (08/2012 - 08/2015)

Outstanding teaching assistant award for Biochemistry courses in 2004-2005, Graduate Division

University of California (01/2004 - 12/2005)

Chemistry departmental scholarship

California State Polytechnic University

SEES departmental scholarship

California State Polytechnic University

California State University Pre-doctoral Scholar Program

SMDP (Scientist Mentoring and Diversity Program) scholar

Career Development and Mentoring Program

ICDP (International Center for Professional Development) (06/2016 - 06/2017)

Professional Interests

• Membranes and Membrane Proteins
• Molecular Basis of Human Disease and Behavior
• Protein Structure-Function and Protein Folding
• Signal Transduction
• Human
• Mouse and Rat

Professional Statement

DETERMINING THE ROLE OF GPCR SIGNALING PROTEINS ON THE ACTIVITY OF THE METABOTROPIC GLUTAMATE RECEPTOR, MGLUR6

Sara Wright, Theodore G. Wensel

Metabotropic glutamate receptors (mGluRs) are G-protein coupled receptors (GPCRs) that are responsible for sensing the neurotransmitter glutamate in the brain, retina, and other CNS tissues. In the retina, G protein signaling is crucial for detection and processing of light. Photons are sensed by the GPCR rhodopsin in rod photoreceptors, which leads to a halt in the release of glutamate at the photoreceptor/ON-bipolar cell synapse. ON-bipolar cells sense glutamate through the metabotropic glutamate receptor mGluR6. In the dark, photoreceptor cells release glutamate, which binds to mGluR6 and activates G protein signaling through G alpha o. This pathway is negatively regulated by RGS7 and RGS11, which are members of the R7 family of regulator of G protein signaling (RGS) proteins. It has been recently determined that the membrane localization of RGS7 is dependent on the orphan receptors GPR158 and GPR179. This project involves determining the effects of RGS7, GPR158, and other potential pathway players on the activity of mGluR6. Assays of mGluR6 activity will be done in cell culture using the FLIPR membrane potential assay. This assay detects changes in membrane potential in response to ion channel activation. Previous results have shown that this assay can be used to determine mGluR6 activity. In addition, localization of the pathway players will be studied in these cells using Immuno-fluorescence, as well as in retina and brain slices.

Websites

Selected Publications

• Melina A. Agosto, Zhixian Zhang, Feng He, Ivan A. Anastassov, Sara J. Wright, Jennifer McGehee, and Theodore G. Wensel "." J Biol Chem. 2014 Sep 26;289(39):27019-33. Pubmed PMID:
• Carla J. Eaton, Ilva E. Cabrera, Jacqueline A. Servin, Sara J. Wright, Murray P. Cox, and Katherine A. Borkovich "." PLOS ONE. 2012;7(10):e48026. Pubmed PMID:
• Hyojeong Kim, Sara J. Wright, Gyungsoon Park, Svetlana Krystofova, and Katherine A. Borkovich "." Genetics. 2012 Apr;190(4):1389-404. Pubmed PMID:
• Sara J. Wright, Regina Inchausti, Carla J. Eaton, Svetlana Krystofova, and Katherine A. Borkovich "." Genetics. 2011 Sep;189(1):165-167. Pubmed PMID: