Gabriele has a strong background in both physics and molecular biology and, accordingly, he strives in interdisciplinary environments. After completing a cum laude BSc. and MSc. in Nanobiology at the Technical University of Delft in The Netherlands, Gabriele pursued a PhD at the University of Copenhagen under the supervision of Prof. Dimitrios Stamou. In his PhD, Gabriele studied the nanoscale spatial organization of G protein-coupled receptors (GPCRs) at the plasma membrane of living cells. Importantly, his work reveals heterogeneous spatial patterns of receptor density and activation, that are modulated in a drug-dependent manner. These findings identify GPCR spatial organization as an integral element of their activity and signaling. Currently, Gabriele is a Postdoctoral Fellow in the lab of Prof. Alice Ting developing programmable receptors for molecular sensing and controlling cellular behaviour.

Professional Education

  • Master of Science, Technische Universiteit Delft (2019)
  • Bachelor of Science, Technische Universiteit Delft (2017)
  • Doctor of Philosophy, University of Copenhagen (2024)
  • BSc, Technical University of Delft, The Netherlands, Nanobiology (2017)
  • MSc, Technical University of Delft, The Netherlands, Nanobiology (2019)
  • PhD, University of Copenhagen (with Dimitrios Stamou), Denmark, Biophysics (2024)

Stanford Advisors

Lab Affiliations

All Publications

  • Molecular mechanism of GPCR spatial organization at the plasma membrane. Nature chemical biology Kockelkoren, G., Lauritsen, L., Shuttle, C. G., Kazepidou, E., Vonkova, I., Zhang, Y., Breuer, A., Kennard, C., Brunetti, R. M., D'Este, E., Weiner, O. D., Uline, M., Stamou, D. 2024; 20 (2): 142-150


    G-protein-coupled receptors (GPCRs) mediate many critical physiological processes. Their spatial organization in plasma membrane (PM) domains is believed to encode signaling specificity and efficiency. However, the existence of domains and, crucially, the mechanism of formation of such putative domains remain elusive. Here, live-cell imaging (corrected for topography-induced imaging artifacts) conclusively established the existence of PM domains for GPCRs. Paradoxically, energetic coupling to extremely shallow PM curvature (<1 µm-1) emerged as the dominant, necessary and sufficient molecular mechanism of GPCR spatiotemporal organization. Experiments with different GPCRs, H-Ras, Piezo1 and epidermal growth factor receptor, suggest that the mechanism is general, yet protein specific, and can be regulated by ligands. These findings delineate a new spatiomechanical molecular mechanism that can transduce to domain-based signaling any mechanical or chemical stimulus that affects the morphology of the PM and suggest innovative therapeutic strategies targeting cellular shape.

    View details for DOI 10.1038/s41589-023-01385-4

    View details for PubMedID 37460675

    View details for PubMedCentralID PMC10792125

  • WASP integrates substrate topology and cell polarity to guide neutrophil migration. The Journal of cell biology Brunetti, R. M., Kockelkoren, G., Raghavan, P., Bell, G. R., Britain, D., Puri, N., Collins, S. R., Leonetti, M. D., Stamou, D., Weiner, O. D. 2022; 221 (2)


    To control their movement, cells need to coordinate actin assembly with the geometric features of their substrate. Here, we uncover a role for the actin regulator WASP in the 3D migration of neutrophils. We show that WASP responds to substrate topology by enriching to sites of inward, substrate-induced membrane deformation. Superresolution imaging reveals that WASP preferentially enriches to the necks of these substrate-induced invaginations, a distribution that could support substrate pinching. WASP facilitates recruitment of the Arp2/3 complex to these sites, stimulating local actin assembly that couples substrate features with the cytoskeleton. Surprisingly, WASP only enriches to membrane deformations in the front half of the cell, within a permissive zone set by WASP's front-biased regulator Cdc42. While WASP KO cells exhibit relatively normal migration on flat substrates, they are defective at topology-directed migration. Our data suggest that WASP integrates substrate topology with cell polarity by selectively polymerizing actin around substrate-induced membrane deformations in the front half of the cell.

    View details for DOI 10.1083/jcb.202104046

    View details for PubMedID 34964841

    View details for PubMedCentralID PMC8719638