Professional Education

  • Bachelor of Science, Sabanci University (2009)
  • Doctor of Philosophy, Carnegie Mellon University (2015)

Stanford Advisors

All Publications

  • Palmitoylation targets the calcineurin phosphatase to the phosphatidylinositol 4-kinase complex at the plasma membrane. Nature communications Ulengin-Talkish, I., Parson, M. A., Jenkins, M. L., Roy, J., Shih, A. Z., St-Denis, N., Gulyas, G., Balla, T., Gingras, A., Varnai, P., Conibear, E., Burke, J. E., Cyert, M. S. 2021; 12 (1): 6064


    Calcineurin, the conserved protein phosphatase and target of immunosuppressants, is a critical mediator of Ca2+ signaling. Here, to discover calcineurin-regulated processes we examined an understudied isoform, CNAbeta1. We show that unlike canonical cytosolic calcineurin, CNAbeta1 localizes to the plasma membrane and Golgi due to palmitoylation of its divergent C-terminal tail, which is reversed by the ABHD17A depalmitoylase. Palmitoylation targets CNAbeta1 to a distinct set of membrane-associated interactors including the phosphatidylinositol 4-kinase (PI4KA) complex containing EFR3B, PI4KA, TTC7B and FAM126A. Hydrogen-deuterium exchange reveals multiple calcineurin-PI4KA complex contacts, including a calcineurin-binding peptide motif in the disordered tail of FAM126A, which we establish as a calcineurin substrate. Calcineurin inhibitors decrease PI4P production during Gq-coupled GPCR signaling, suggesting that calcineurin dephosphorylates and promotes PI4KA complex activity. In sum, this work discovers a calcineurin-regulated signaling pathway which highlights the PI4KA complex as a regulatory target and reveals that dynamic palmitoylation confers unique localization, substrate specificity and regulation to CNAbeta1.

    View details for DOI 10.1038/s41467-021-26326-4

    View details for PubMedID 34663815

  • Uncovering The Unique Functions And Regulation Of The Palmitoylated Calcineurin Isoform, CN beta 1 Ulengin-Talkish, I., Bond, R., St-Denis, N., Gingras, A., Shih, A., Conibear, E., Balla, T., Varnai, P., Cyert, M. WILEY. 2020