A postdoctoral research position is available at the Kiyokawa lab (https://sites.northwestern.edu/kiyokawalab/) to investigate roles of ubiquitination enzymes in neurological disorders and develop small molecule modulators of disease-associated ubiquitin ligases. We are located on Northwestern’s medical campus in the nice safe neighborhood of downtown Chicago.
The Kiyokawa lab has been studying over two decades the molecular, biological and translational properties of posttranslational modifications of cellular proteins, especially phosphorylation and ubiquitination, and their involvement in human diseases. Our current goal is to develop novel therapeutic strategies to target protein ubiquitination in patients with cancer, neurodevelopmental and neurodegenerative disorders. We use diverse experimental model systems such as induced pluripotent stem cells (iPSC) combined with CRISPR/Cas9 gene editing, a novel proteomic screening platform called Orthogonal Ubiquitin Transfer (OUT), small molecule screens for ubiquitination modifiers, and genetically engineered mouse models. Our recent publications are available from the following link (https://sites.northwestern.edu/kiyokawalab/publications/).
About the position:
Autism-spectrum disorders (ASD) are highly prevalent neurodevelopmental diseases, and mechanism-based therapies are urgently needed. Dysfunction of the UBE3A gene encoding a ubiquitin ligase is one of the highest-confidence genetic cause of ASD (https://gene.sfari.org). We have recently established the novel proteomic technology OUT to identify substrate proteins of UBE3A-mediated ubiquitination (https://www.nature.com/articles/s41467-017-01974-7). This position is to identify neuron-specific UBE3A substrates by applying this method to iPSC-derived neurons, reveal their roles in the pathogenesis of ASD using iPSC and mouse models, and develop new therapeutic strategies for ASD. The work will be conducted in a multidisciplinary and collaborative network within and beyond the Northwestern community.