Research Group: Plant Signaling

We study different component of signaling, including H+ and Ca2+ fluxes, activation of protein kinases and phosphatases, and signalling peptides and their receptors.

Signal perception at the cell surface by receptors and transduction of these signals to the cell interior is essential for plants in order to react and adapt to changes in the surroundings.

Studies of signal transduction and receptor activation that together modulate growth and development is a complex, but fascinating topic. This work requires a combination of biochemical, molecular and bioimaging methods.

Another interest is plant and fungal receptors for bacterial outer cell wall molecules, the following signaling pathways in eukaryotic hosts, and the chemical structures and synthesis of some of these bacterial molecules.

Finally, an applied angle of the research is identification of modulators of both plant and fungal H+-ATPases, as these proteins has a great potential as growth regulator- and drug-targets. Here we have recently performed a systematic screening of fungal compounds for their effect on the plant PM H+-ATPase enzyme activity. This have led to the identification of several compounds with a biotechnological potential as “Plant Biologicals”.

Find more information about the group in the menu below.









Fungal pathogens secrete hundreds of effector proteins to promote disease. By using a yeast-based screen, we aim at identifying molecular effector targets and elucidate the mechanism of the effectors. Identification of effector mechanisms will be used in the development of crops with improved resistance towards pathogens.

Naturlige vækststimulerende plantepeptider - produktion og test på næringsstofoptag
The purpose of this project is to produce small sulfated plant peptides in yeast and evaluate their potential as new plant growth promoting peptides.

Nanodisc production in living cells facilitates structural studies of membrane proteins
Willum experiment to Frederik Tidemand (2022-2023).

Direct extraction of active membrane proteins and complexes for cryo-EM
Willum experiment to Nicolai Johansen (2021-2022).






Screening for modulators of H+-ATPase activity:

Tenuazonic acid from Stemphylium loti inhibits the plant plasma membrane H+ -ATPase by a mechanism involving the C-terminal regulatory domain.

Bjørk PK, Rasmussen SA, Gjetting SK, Havshøi NW, Petersen TI, Ipsen JØ, Larsen TO, Fuglsang AT.

New Phytol. (2020)

Identification of Antifungal H+-ATPase Inhibitors with Effect on Plasma Membrane Potential.

Kjellerup L, Gordon S, Cohrt KO, Brown WD, Fuglsang AT, Winther AL.

Antimicrob Agents Chemother. (2017)


Peptide-Receptor signaling:

Evidence for multiple receptors mediating RALF-triggered Ca2+ signaling and proton pump inhibition.

Gjetting SK, Mahmood K, Shabala L, Kristensen A, Shabala S, Palmgren M, Fuglsang AT.

Plant J. (2020)

Activation of the LRR Receptor-Like Kinase PSY1R Requires Transphosphorylation of Residues in the Activation Loop.

Oehlenschlæger CB, Gersby LBA, Ahsan N, Pedersen JT, Kristensen A, Solakova TV, Thelen JJ, Fuglsang AT.

Front Plant Sci. (2017)


Proton and calcium pumping P-type ATPases and their regulation of plant responses to the environment, Anja T Fuglsang, Michael Palmgren, Plant Physiology, (2020)

A critical review on natural compounds interacting with the plant plasma membrane H+ -ATPase -and their potential as biologicals in agriculture.

Havshøi NW, Fuglsang AT. J Integr Plant Biol. (2022)



Group members

Name Title Phone E-mail
Amalie Scheel Tost PhD Fellow   E-mail
Anja Thoe Fuglsang Professor +4535332586 E-mail
Barbara Dusak PhD Fellow +4535336410 E-mail
Frederik Grønbæk Tidemand Postdoc +4528257092 E-mail
Marzanna Due Laboratory Technician +4535328186 E-mail
Nanna Weise Havshøi PhD Fellow +4535325140 E-mail
Nicolai Tidemand Johansen Postdoc +4535337967 E-mail
Rui Wu Postdoc +4535327113 E-mail

Master students

  • Gustav Søndergaard Nymand
  • Lei Li

Contact research group leader

Professor Anja Thoe FuglsangAnja Thoe Fuglsang
Ph: +45 35 33 25 86