skip to content

Leidecker lab - Institute for Genetics

Mapping PTMs and Proteins that Regulate Nucleoporin Dynamics at the Nuclear Pore Complex

Project of the 2nd cohort:

ADP-ribosylation (ADPr) is a posttranslational modification (PTM) catalysed by poly-ADP-ribose polymerases (PARPs) such as PARP11 and involves the transfer of ADP-ribose moieties to proteins using NAD+ as a donor. PARP11 has recently been found to play a regulatory role in innate immunity and is a potential novel immuno-oncology target. Interestingly, the long canonical isoform of PARP11 localises to the nuclear pore complex (NPC) in a catalytic activity dependent manner, while the short isoform lacking the WWE domain fails to localise the the NPC. Which isoform is involved in the regulation of innate immunity is unclear, however, the dual localisation of PARP11 suggests its potential to regulate the NPC by ADPr. The overarching goal of this project is to determine the functional consequences of PARP11 perinuclear localization and ADPr activity on NPC biology and its impacts on health and disease.


Project of the 3rd cohort:

The nuclear pore complex (NPC) is embedded in the nuclear membrane and consists of 34 nucleoporins (Nup) that govern nucleocytoplasmic transport and play a pivotal role in precisely regulating cellular homeostasis. Peripheral Nups, such as Nup153 and ELYS display dynamic association to the NPC, and are important regulators of NPC assembly.

In this project, we will determine which PTMs and binding partners contribute to interphase and post-mitotic NPC assembly and influence the dynamic relocalization of Nup153 and ELYS between the complex and the nucleoplasm, using proteomics and live-cell imaging approaches.


Jessica Wirtz

PhD Student since January 2024

EMail: jwirtz9[at]

"I completed my Bachelor's and Master's degrees in Biological Sciences at the University of Cologne. During my studies I gained insight into immunofluorescence imaging and proteomics. In the Leidecker lab, I'm currently working on the intricacies of PARP11, an enzyme involved in ADP-ribose transfer. Using techniques such as immunofluorescence imaging and proteomics, I'm investigating its localisation and role at the nuclear envelope. My research aims to provide new insights into cellular processes and potential therapeutic avenues."