Combining state of the art with traditional microscopy at Octopus reveals new insights into protein function regulation
08 Jul 2022
- Mathew Sims



Research combining the newest technique available at Octopus with one of the oldest, to investigate a novel interaction between proteins, has just been published online ahead of full publication in the Structure journal.

A diagram of FLRT protein interactions, taken from the research paper.

​A diagram of FLRT protein interactions, taken from the research paper.


Fibronectin Leucine-rich Repeat Transmembrane (FLRT 1–3) proteins are important in neural, vascular, and embryonic development. Single Molecule Tracking enabled researchers to watch pairs of fluorescently tagged FLRT proteins moving together across the surface of live cells. MINFLUX, a state-of-the-art super resolution microscope recently installed at OCTOPUS was then used to measure the separations of these pairs with near nanometre precision, in fixed cells.

The research was conducted by Octopus scientists Chris Tynan, Dan Rolfe and Marisa Martin-Fernandez and the group of CLF user Elena Seiradake from the University of Oxford, in collaboration with Matthieu Chavent and colleagues from l'Institut de pharmacologie et de biologie structural (IPBS) in Toulouse, University of Leeds Institute of Cardiovascular and Metabolic Medicine, and the Wellcome Centre for Human Genetics at the University of Oxford.

MINFLUX found that, on average, the proteins were 10 nm apart, which is close enough to be interacting directly with each other.

The experimental results from the CLF, combined with molecular dynamics simulations carried out in Oxford and Toulouse, suggest the new interaction could be a versatile way of regulating the functions of the protein and help explain how they can regulate such a diverse range of processes.

Read the paper at

Contact: Sims, Mathew (STFC,RAL,SC)