Transmission electron microscopy imaging showing in detail Nuclear Pores (NPC) in the nuclear envelope of tumor cells. Red arrow points one NPC. Scale bar 1uM (Top left). Cartoon depicting Nuclear Pore Complex and listing its protein components, nucleoporins (NUPs) (Top right). Fluorescence microscopy images of mitotic protein Mad1 localization to nuclear pores.  Magnified images show in detail colocalization of Mad1 with a NPC marker. (Green, Mad1; Red, NPC; blue,DNA). (Rodriguez-Bravo Lab images).

the molecular level in cancer cells and preclinical models.Our group is performing comprehensive studies interrogating the specific NUP-regulated molecular mechanisms that contribute to tumor cells aggressiveness. Integrating transcriptomics, genetics, cell biology approaches and validation in patient tumor samples we aim to decipher potential new mechanisms with an important role in cancer. We recently led a study unveiling a novel mechanisms by which NPC composition changes fuel Prostate Cancer progression (Rodriguez-Bravo et al. Cell 2018).

Nuclear Pore Complex and Cancer

Our Lab is studying how deregulation of Nuclear Pores impact cancer cells and contributes to aggressive phenotypes. NPC defects have been identified in a variety of human cancers and linked to oncogenesis however their mechanistic contribution to cancer pathogenesis is not well understood. These nucleocytoplasmic gateways perforate the nuclear envelope and control selective transport of molecules between the nucleus and the cytoplasm. However, The NPC components, called nucleoporins (NUPs), have been involved in many other essential biological processes such as genome integrity, chromatin organization or gene expression.

Previous work described the cooperation between mitotic proteins and Nuclear Pore complex (NPC) components, nucleoporins, to ensure robustness of the Spindle Assembly Checkpoint and ultimately protecting genome stability (Rodriguez-Bravo et all Cell 2014). We are further elucidating these pathways at