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
Heterophilic interactions between cell-surface proteins Teneurin-m and Capricious drive dendrite segregation in the Drosophila olfactory circuit.
Heterophilic interactions between cell-surface proteins Teneurin-m and Capricious drive dendrite segregation in the Drosophila olfactory circuit. Curr Biol. 2026 Sep 21.
PMID: 42767218
The teneurin TEN-1 and its ligand LRON-11 support microbiota-induced neuroprotection and mechanosensory function in C. elegans.
The teneurin TEN-1 and its ligand LRON-11 support microbiota-induced neuroprotection and mechanosensory function in C. elegans. Curr Biol. 2026 Sep 21.
PMID: 42767219
Reexamining the activation mechanisms of adhesion G protein-coupled receptors.
Reexamining the activation mechanisms of adhesion G protein-coupled receptors. Sci Signal. 2026 Sep; 19(953):eaeg6095.
PMID: 42679016
Ligand-tuned extracellular domain dynamics are correlated with signaling states in an adhesion GPCR.
Ligand-tuned extracellular domain dynamics are correlated with signaling states in an adhesion GPCR. Sci Adv. 2026 Aug 14; 12(33):eaea8715.
PMID: 42599991
Adhesion G protein-coupled receptors.
Adhesion G protein-coupled receptors. Pharmacol Rev. 2026 May; 78(3):100116.
PMID: 41895071
Synaptic Cell Adhesion: A Structural Perspective.
Synaptic Cell Adhesion: A Structural Perspective. Adv Neurobiol. 2026; 48:151-190.
PMID: 41569485
The far extracellular CUB domain of the adhesion GPCR ADGRG6/GPR126 is a key regulator of receptor signaling.
The far extracellular CUB domain of the adhesion GPCR ADGRG6/GPR126 is a key regulator of receptor signaling. Proc Natl Acad Sci U S A. 2025 Dec 02; 122(48):e2409184122.
PMID: 41296714
Structural basis and functional roles for Toll-like receptor binding to Latrophilin in C.?elegans development.
Structural basis and functional roles for Toll-like receptor binding to Latrophilin in C.?elegans development. Nat Struct Mol Biol. 2025 Sep; 32(9):1683-1696.
PMID: 40588662
Structural basis for regulation of CELSR1 by a compact module in its extracellular region.
Structural basis for regulation of CELSR1 by a compact module in its extracellular region. Nat Commun. 2025 Apr 28; 16(1):3972.
PMID: 40295529
Conformational coupling between extracellular and transmembrane domains modulates holo-adhesion GPCR function.
Conformational coupling between extracellular and transmembrane domains modulates holo-adhesion GPCR function. Nat Commun. 2024 12 04; 15(1):10545.
PMID: 39627215
Catalyst Award
Chicago Biomedical Consortium
2019 - 2021
Distinguished Investigator
University of Chicago
2019
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