Research group of Jörg Großhans

Institute of Developmental Biochemistry
Georg-August-Universität Göttingen











13.4.18 Anja's review in JCS is available now

13.1.18 Roman's EM study is now in press

22.12.17 Zhiyi's guillotine paper is in press

19.12.17 Anja's and Zhiyi's ELMO/Canoe paper is in press

17.12.17 Roman's NUCLEUS paper is in press

18.11.17 SLAM paper of Shuling et al is in press with PlosBiology

Structure formation in early Drosophila embryos

Research topics

Epithelial morphogenesis and cell cycle switch

- Membrane and epithelial compartment formation
- Actin dynamics and Rho signalling
- Role of the slam RNA-protein complex
- Cell cycle control

Quantitative morphogenesis (Biomechanics)

- Nuclear ordering and cytoskeletal network dynamics
- Cell intercalation and junction dynamics

Size and form of the nucleus - Ageing

- Farnesylated nuclear lamina proteins
- Drosophila model for the Hutchinson-Gilford progeria (HGPS) and other laminopathies
- Lamina proteins in regeneration and proliferation of intestinal stem cells


- Drosophila genetics, embryology, adult ageing
- Molecular genetics
- Biochemistry
- Classical and quantitative microscopy and live imaging
- Micro-surgery with UV laser
- Computational image analysis

Cross-section of an embryo during early gastrulation. Adherens junctions (red), RhoGEF2 (green), DNA (blue). Ventral cells show specific cell behaviour, in that they change their shape initiated by apical constriction triggered by relocalisation of RhoGEF2 from basal to apical.

kugelkern mutant embryos do not elongate their nuclei during cellularisation, leaving them sperical. Consitent with its function the Kugelkern protein is associated with the inner nuclear membrane similar to lamina proteins. Similar to LaminDmO Kugelkern is farnesylated at its C-terminus what promotes membrane association. Immunofluorescence and immuno-electron microscopy in which Kugelkern is marked by 10 nm Gold particles.