Structural and functional characterization of annexin 1 from Medicago truncatula

Praveen Kumar Kodavali, Krzysztof Skowronek, Izabela Koszela-Piotrowska, Agnieszka Strzelecka-Kiliszek, Krzysztof Pawlowski, Slawomir Pikula

Research output: Contribution to journalArticlepeer-review

11 Scopus citations


Annexins are calcium- and membrane-binding proteins that have been shown to have diverse properties such as actin, integrin and GTP binding, both in animals and plants. Recently, Medicago truncatula annexin 1 (AnnMt1) has been suggested to participate in nodulation (Nod factor signaling) and mycorrhization in legume plants. In this report we demonstrate for the first time that recombinant AnnMt1 (rec-AnnMt1) mediates membrane permeabilization to cations with conductance ranging from 16pS to 329pS. In agreement with other structurally determined annexins, homology modeling of AnnMt1 suggests that most of the functional determinants are found on the convex surface of the modeled structure. In conclusion, we propose a potential constitutive role of AnnMt1 in Nod factor signaling as a non-specific ion channel.

Original languageEnglish (US)
Pages (from-to)56-62
Number of pages7
JournalPlant Physiology and Biochemistry
StatePublished - Dec 2013
Externally publishedYes


  • Annexin 1
  • Ion channel
  • Medicago truncatula
  • Protein structure

ASJC Scopus subject areas

  • Physiology
  • Genetics
  • Plant Science


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