Plant Cell Reports

, Volume 37, Issue 4, pp 627–639 | Cite as

In silico identification and experimental validation of amino acid motifs required for the Rho-of-plants GTPase-mediated activation of receptor-like cytoplasmic kinases

  • Dézi Bianka Lajkó
  • Ildikó Valkai
  • Mónika Domoki
  • Dalma Ménesi
  • Györgyi Ferenc
  • Ferhan Ayaydin
  • Attila Fehér
Original Article


Key message

Several amino acid motifs required for Rop-dependent activity were found to form a common surface on RLCKVI_A kinases. This indicates a unique mechanism for Rho-type GTPase-mediated kinase activation in plants.


Rho-of-plants (Rop) G-proteins are implicated in the regulation of various cellular processes, including cell growth, cell polarity, hormonal and pathogen responses. Our knowledge about the signalling pathways downstream of Rops is continuously increasing. However, there are still substantial gaps in this knowledge. One reason for this is that these pathways are considerably different from those described for yeast and/or animal Rho-type GTPases. Among others, plants lack all Rho/Rac/Cdc42-activated kinase families. Only a small group of plant-specific receptor-like cytoplasmic kinases (RLCK VI_A) has been shown to exhibit Rop-binding-dependent in vitro activity. These kinases do not carry any known GTPase-binding motifs. Based on the sequence comparison of the Rop-activated RLCK VI_A and the closely related but constitutively active RLCK VI_B kinases, several distinguishing amino acid residues/motifs were identified. All but one of these were found to be required for the Rop-mediated regulation of the in vitro activity of two RLCK VI_A kinases. Structural modelling indicated that these motifs might form a common Rop-binding surface. Based on in silico data mining, kinases that have the identified Rop-binding motifs are present in Embryophyta but not in unicellular green algae. It can, therefore, be supposed that Rops recruited these plant-specific kinases for signalling at an early stage of land plant evolution.


Arabidopsis thaliana Cellular signalling, kinase activity Protein–protein interaction RLCK Rop GTPase 



This work was supported by grants from the National Research, Development, and Innovation Office (NKFIH; #K101112) and the Hungarian Ministry for National Economy (GINOP-2.3.2-15-2016-00001).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

299_2018_2256_MOESM1_ESM.pptx (191 kb)
Supplementary material 1 (PPTX 191 KB)
299_2018_2256_MOESM2_ESM.xlsx (11 kb)
Supplementary material 2 (XLSX 11 KB)


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Copyright information

© Springer-Verlag GmbH Germany, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Biological Research Centre, Institute of Plant BiologyHungarian Academy of SciencesSzegedHungary
  2. 2.Department of Plant BiologyUniversity of SzegedSzegedHungary

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