Skip to main content English


Roland Foisner
Roland Foisner, o.Univ.Prof. Dr.

Center for Medical Biochemistry (Division of Molecular Biology)
Position: Professor

ORCID: 0000-0003-4734-4647
T +43 1 4277 61680

Further Information


Adult Stem Cells; Aging, Premature; Cardiovascular Diseases; Chromatin; Epigenomics; Lamin Type A; Muscular Dystrophies; Nuclear Envelope; Nuclear Lamina

Research interests

Lamins in nuclear organization and human disease

Lamins form a scaffold structure at the nuclear envelope, the lamina,  and are also found throughout the nucleoplasm. They determine mechanical properties of the nucleus and are involved in chromatin regulation. Lamin mutations cause human diseases ranging from muscular dystrophy to premature-aging syndromes.

We aim at understanding molecular mechanisms of lamin functions in nuclear organization and chromatin regulation during differentiation and their role in diseases. In particular, we investigate i) how lamin-binding proteins affect lamin dynamics and functions, ii) how these proteins crontrol lamin-chromatin interactions, and iii) how these processes are affected by lamin disease mutations.

While lamin-chromatin interactions are known to contribute to stable gene repression during differentiation, we found binding of lamins also to active, open chromatin throughout the nucleus, affecting epigenetic pathways and gene regulation. This activity is changed in cells expressing a progeria premature ageing disease-linked lamin mutant.

A second focus in the lab addresses molecular pathways causing cardiovascular disease in progeria premature aging disease. In mouse models expressing the lamin disease variant in endothelial cells, we investigate pro-atherogenic changes at the molecular level.    

Techniques, methods & infrastructure

We use transgenic mouse models, primary cells and patient cells to study the molecular functions of lamins in cell differentiation and tissue homeostasis as well as molecular disease mechanisms leading to muscular dystrophy and cardiovascular disease in Emery Dreifuss Muscular Dystrophy (EDMD) and progeria patients.

Selected publications

  1. Gesson, K. et al., 2016. A-type lamins bind both hetero- and euchromatin, the latter being regulated by lamina-associated polypeptide 2 alpha. Genome Research, 26(4), pp.462-473. Available at:
  2. Vidak, S. et al., 2015. Proliferation of progeria cells is enhanced by lamina-associated polypeptide 2α (LAP2α) through expression of extracellular matrix proteins. Genes & Development, 29(19), pp.2022-2036. Available at:
  3. Bronshtein, I. et al., 2015. Loss of lamin A function increases chromatin dynamics in the nuclear interior. Nature Communications, 6, p.8044. Available at:
  4. Naetar, N. et al., 2008. Loss of nucleoplasmic LAP2α-lamin A complexes causes erythroid and epidermal progenitor hyperproliferation. Nature Cell Biology, 10(11), pp.1341-1348. Available at:
  5. Dorner, D. et al., 2006. Lamina-associated polypeptide 2α regulates cell cycle progression and differentiation via the retinoblastoma-E2F pathway. The Journal of Cell Biology, 173(1), pp.83-93. Available at: