Proteomic signatures implicate cAMP in light and temperature responses in Arabidopsis thaliana

Ludivine Thomas, Claudius Marondedze, Luisa Ederli, Stefania Pasqualini, Christoph A Gehring

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

The second messenger 3'-5'-cyclic adenosine monophosphate (cAMP) and adenylyl cyclases (ACs), enzymes that catalyse the formation of cAMP from ATP, are increasingly recognized as important signaling molecules in a number of physiological responses in higher plants. Here we used proteomics to identify cAMP-dependent protein signatures in Arabidopsis thaliana and identify a number of differentially expressed proteins with a role in light- and temperature-dependent responses, notably photosystem II subunit P-1, plasma membrane associated cation-binding protein and chaperonin 60 β. Based on these proteomics results we conclude that, much like in cyanobacteria, algae and fungi, cAMP may have a role in light signaling and the regulation of photosynthesis as well as responses to temperature and we speculate that ACs could act as light and/or temperature sensors in higher plants. Biological significance: This current study is significant since it presents the first proteomic response to cAMP, a novel and key second messenger in plants. It will be relevant to researchers in plant physiology and in particular those with an interest in second messengers and their role in biotic and abiotic stress responses. © 2013 Elsevier B.V.
Original languageEnglish (US)
Pages (from-to)47-59
Number of pages13
JournalJournal of Proteomics
Volume83
DOIs
StatePublished - May 2013

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics

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