Research interests in our research group

Our group is interested in how the actin cross-linking protein filamin regulates cell adhesion and differentiation.
Filamins are large proteins with diverse functions. They link actin filaments to networks, anchor plasma membrane receptors to the cytoskeleton, and have a scaffolding function in signaling. There are three filamin genes in the human genome. Filamin A and Filamin B are ubiquitously expressed, whereas Filamin C is muscle-specific. Mutations in the Filamin A gene lead to a neuronal defect called periventricular heterotopia. Patients carrying Filamin A mutations also frequently suffer from gut, bone and cardiovascular abnormalities. Mutations in the Filamin B gene lead to bone abnormalities. Many of these may have something to do with cell migration during development. In cell culture models, Filamin interactions with the integrin family of cell adhesion receptors regulate cell migration.

Selected publications

Green, H.J., Griffiths, A.G.M., Ylänne, J., and Brown, N.H. (2018). Novel functions for integrin-associated proteins revealed by analysis of myofibril attachment in Drosophila. ELife 7, e35783.

Huelsmann, S., Rintanen, N., Sethi, R., Brown, N.H., and Ylänne, J. (2016). Evidence for the mechanosensor function of filamin in tissue development. Sci. Rep. 6, srep32798.

Rognoni L., Stigler J., Pelz B., Ylänne J. and Rief M. 2012. Dynamic force sensing of filamin revealed in single-molecule experiments. Proc. Natl. Acad. Sci. U S A. 109:19679-19684

Kiema T., Lad Y., Jiang P., Oxley C. L., Baldassarre M., Wegener K. L., Campbell I. D. , Ylänne J., and Calderwood D. A. 2006. Structure of a filamin-integrin complex reveals the molecular basis of binding and competition with talin. Mol. Cell 21: 337-347.