My lab investigates key regulatory circuits that control the host inflammatory response, with a special emphasis on the complex molecular mechanisms and signaling events that lead to changes in cellular structure and function.


Receptors on the cell surface sense and respond to extracellular ligands and transmit the signals to the cell interior. Here, signal transduction pathways elicited through G-protein-coupled receptors (GPCRs), and the functional analysis of the Pattern Recognition Receptors, is a key aspect of our work (Pupjalis et al.; EMBO Mol. Med. 2011). Another major research topic is the late endosome, and its function as an important hub for the segregation of incoming cargo (Poeter et al.; Nature Commun. 2014) and as site of the endosomal escape for enveloped viruses (Kühnl et al.; mBio 2018), in particular Influenza A (in close cooperation with the Institute of Virology).





We are part of the SFB 1009 Breaking Barriers and SFB 1348 Dynamic Cellular Interfaces


Women in Science
26.-27. November


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Targeting cellular cholesterol levels may help fight the flu

*To fight against the flu, vaccines are prepared from virus strains that resemble those that are likely to circulate in the upcoming influenza season. However, protection by vaccination is limited due to the abrupt and unpredictable emergence of new subtypes that may rapidly spread worldwide. Therefore, drugs that target host cell factors could open up efficient therapeutic strategies to keep viruses from reproducing in the body. We found that host cell factors involved in maintaining proper cholesterol homeostasis such as AnxA6 have a major impact on IAV replication. AnxA6 indirectly regulates IAV replication via reducing the availability of cholesterol at the plasma membrane, thereby equipping the budding virus with an envelope that is strongly reduced in cholesterol (see our new article “Annexin A6-balanced late endosomal cholesterol controls influenza A replication and propagation” for more information). Thus, targeting the cellular cholesterol balance might ameliorate IAV infection.

Musiol A, Gran, Ehrhardt C, Ludwig S, Grewal T, Gerke V, Rescher U. mBio 2013.



In a dark place

To keep everything neat, tidy, and organized, the eukaryotic cell relies on an intricate system of distinct compartments. But the large nucleus of a mammalian cell sticks to that routine, too. It features a complex internal structure with a variety of specific subnuclear bodies, including the not so well known paraspeckles. These quite recently discovered ribonucleoprotein bodies are formed by the assembly of paraspeckle proteins and specific long non-coding RNAs transcribed by Pol II. Paraspeckles might serve as retention sites for otherwise transcription-competent RNA, thereby adding a new layer of complexity to the complicated posttranscriptional control of gene expression. While working on the cellular functions of atypical annexins, we found to our surprise that annexin A10 co-localizes with the mRNA-binding proteins SFPQ and PSPC1 at paraspeckles, and decreases paraspeckle numbers when overexpressed in HeLa cells. In addition, annexin A10 relocates to Dark Nucleolar Caps upon transcriptional inhibition of RNA polymerase II, a typical behavior of paraspeckle proteins. For more information, read our article published in Cellular and Molecular Life Sciences.

Quiskamp N, Poeter M, Raabe CA, Hohenester UM, König S, Gerke V, Rescher U. Cell Mol Life Sci. 2013 May 29. [Epub ahead of print]


In control of mitogenic signaling

Mitogenic Epidermal Growth Factor (EGF) signaling controls complex intracellular pathways involved in cell growth and differentiation. Activated EGF receptors are internalized and degraded in lysosomes to prevent chronic stimulation leading to tumor formation and progression.

We published a new article on the control of EGFR signal duration in Biochimica et Biophysica Acta (BBA)-Molecular Cell Research. The title is “Disruption of the annexin A1/S100A11 complex increases the migration and clonogenic growth by dysregulating epithelial growth factor (EGF) signaling”. Together with colleagues from the University of Sydney we provide evidence that complex formation of annexin A1 with S100C is essential for proper targeting the EGF receptor to lysosomes, possibly by acting as a physical scaffold that supports formation of inner vesicles in MVBs. Ablation of the complex results in prolonged EGFR signaling and enhanced cell migration and clonogenicity

Biochim Biophys Acta. 2012 Dec 14. pii: S0167-4889(12)00369-2. doi: 10.1016/j.bbamcr.2012.12.006. [Epub ahead of print]



Join us

We have open positions for PhD student positions (Control of the host inflammatory response; Regulation of Membrane trafficking events). Please send your application in English as a single PDF file, containing a cover letter with a statement of research interests, a CV including your research experience, and the contact information of two references.



Contact address


Prof. Dr. Ursula Rescher
Institut für Medizinische Biochemie, ZMBE
Von-Esmarch-Straße 56
D-48149 Münster
phone +49 251 83 52121 / Fax - 56748

e-mail: rescher at