Professional Education

  • Doctor of Philosophy, University of Zurich (2017)
  • Bachelor of Science, Universidad Complutense Madrid (2010)
  • Master of Science, Universidad Complutense Madrid (2012)

Stanford Advisors

Lab Affiliations

All Publications

  • Protein phosphatase 1 regulates core PCP signaling. EMBO reports Song, S., Cho, B., Weiner, A. T., Nissen, S. B., Ojeda Naharros, I., Sanchez Bosch, P., Suyama, K., Hu, Y., He, L., Svinkina, T., Udeshi, N. D., Carr, S. A., Perrimon, N., Axelrod, J. D. 2023: e56997


    Planar cell polarity (PCP) signaling polarizes epithelial cells within the plane of an epithelium. Core PCP signaling components adopt asymmetric subcellular localizations within cells to both polarize and coordinate polarity between cells. Achieving subcellular asymmetry requires additional effectors, including some mediating post-translational modifications of core components. Identification of such proteins is challenging due to pleiotropy. We used mass spectrometry-based proximity labeling proteomics to identify such regulators in the Drosophila wing. We identified the catalytic subunit of protein phosphatase1, Pp1-87B, and show that it regulates core protein polarization. Pp1-87B interacts with the core protein Van Gogh and at least one serine/threonine kinase, Dco/CKI╬Á, that is known to regulate PCP. Pp1-87B modulates Van Gogh subcellular localization and directs its dephosphorylation in vivo. PNUTS, a Pp1 regulatory subunit, also modulates PCP. While the direct substrate(s) of Pp1-87B in control of PCP is not known, our data support the model that cycling between phosphorylated and unphosphorylated forms of one or more core PCP components may regulate acquisition of asymmetry. Finally, our screen serves as a resource for identifying additional regulators of PCP signaling.

    View details for DOI 10.15252/embr.202356997

    View details for PubMedID 37975164

  • Anchor Away: A System for Fast Inhibition of Proteins in Drosophila. Methods in molecular biology (Clifton, N.J.) Sanchez Bosch, P. 2022; 2540: 239-249


    Anchor away is a sequestering method designed to acutely and timely abrogate the function of a protein of interest by anchoring to a cell compartment different from its target. This method induces the binding of the target protein to the anchor by either the addition of rapamycin to Drosophila food or cell media. Rapamycin mediates the formation of a ternary complex between the anchor, which is tagged with the FK506-binding protein (FKBP12), and the target protein fused with the FKB12 rapamycin-binding (FRB) domain of mammalian target of rapamycin (mTOR). The rapamycin-bound target protein stays sequestered away from its compartment, where it cannot perform its biological function.

    View details for DOI 10.1007/978-1-0716-2541-5_11

    View details for PubMedID 35980581