PI last name in publications: ARAÇ 
ARAÇ LAB RESEARCH 
Cells in multicellular organisms have the extraordinary ability of adhering to each other and exchanging information. Cellular adhesion and communication is essential for the development of all organs such as the brain, and is a key phenomenon that is disrupted in many human diseases. The Araç Lab is interested in understanding cellular communication with a special focus on the cell-surface receptors that mediate intercellular adhesion and communication. Genetic studies revealed critical roles for these surface proteins in embryonic development (especially of the brain and the heart), and in neurobiology (especially in synaptogenesis, axon pathfinding, axon-dendrite partner marching and wiring the brain); and link them to numerous diseases including neurological disorders, developmental impairments, multiple types of cancers (such as glioblastoma and ovarian cancer) and congenital general anosmia (the inability to smell). Considering that many drugs target the extracellular regions of membrane receptors to regulate receptor function, and have excellent therapeutic benefits, these proteins may be promising targets for drugs to treat numerous diseases once mechanistic details about the components that regulate their functions are understood. However, in spite of the recent exciting advances, their mechanisms of action, high-resolution structures in isolation or in complex with their ligands, and how they can mediate such broad range of functions remain majorly unknown. Our lab’s ultimate goal is to understand the mechanisms by which cell-adhesion receptors mediate communication between cells.
            Stanford University
            Stanford, CA
            Postdoctoral - Structural and Cellular Biology
            2013          
            UT Southwestern Med. Center
            Dallas, TX
            PhD - Molecular Biophysics
            2006          
            Bilkent University
            Ankara, Turkey 
            BS - Molecular Biology and Genetics
            1999          
            Teneurins and latrophilins: two giants meet at the synapse.
            Teneurins and latrophilins: two giants meet at the synapse. Curr Opin Struct Biol. 2019 02; 54:141-151.
            PMID: 30952063
          
            A Comprehensive Mutagenesis Screen of the Adhesion GPCR Latrophilin-1/ADGRL1.
            A Comprehensive Mutagenesis Screen of the Adhesion GPCR Latrophilin-1/ADGRL1. iScience. 2018 May 25; 3:264-278.
            PMID: 30428326
          
            Structural Basis for Teneurin Function in Circuit-Wiring: A Toxin Motif at the Synapse.
            Structural Basis for Teneurin Function in Circuit-Wiring: A Toxin Motif at the Synapse. Cell. 2018 04 19; 173(3):735-748.e15.
            PMID: 29677516
          
            A new MR-SAD algorithm for the automatic building of protein models from low-resolution X-ray data and a poor starting model.
            A new MR-SAD algorithm for the automatic building of protein models from low-resolution X-ray data and a poor starting model. IUCrJ. 2018 Mar 01; 5(Pt 2):166-171.
            PMID: 29765606
          
            Stachel-independent modulation of GPR56/ADGRG1 signaling by synthetic ligands directed to its extracellular region.
            Stachel-independent modulation of GPR56/ADGRG1 signaling by synthetic ligands directed to its extracellular region. Proc Natl Acad Sci U S A. 2017 09 19; 114(38):10095-10100.
            PMID: 28874577
          
            Structural Basis for Regulation of GPR56/ADGRG1 by Its Alternatively Spliced Extracellular Domains.
            Structural Basis for Regulation of GPR56/ADGRG1 by Its Alternatively Spliced Extracellular Domains. Neuron. 2016 Sep 21; 91(6):1292-1304.
            PMID: 27657451
          
            Understanding the Structural Basis of Adhesion GPCR Functions.
            Understanding the Structural Basis of Adhesion GPCR Functions. Handb Exp Pharmacol. 2016; 234:67-82.
            PMID: 27832484
          
            Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion.
            Structural Basis of Latrophilin-FLRT-UNC5 Interaction in Cell Adhesion. Structure. 2015 Sep 01; 23(9):1678-1691.
            PMID: 26235030
          
            International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G protein-coupled receptors.
            International Union of Basic and Clinical Pharmacology. XCIV. Adhesion G protein-coupled receptors. Pharmacol Rev. 2015; 67(2):338-67.
            PMID: 25713288
          
            New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors.
            New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors. Ann N Y Acad Sci. 2014 Dec; 1333:43-64.
            PMID: 25424900
          
            Fay/Frank Seed Grant
            Brain Research Foundation 
            2014 - 2015          
            Big Ideas Generator 
            University of Chicago
            2014 - 2015          
            Life Sciences Research Foundation Postdoctoral Fellowship
            Howard Hughes Medical Center
            2007 - 2010          
            Chancellor’s Distinguished Fellowship
            University of California, Riverside
            1999 - 2000          
