Abstract

The second messenger 3′,5′-cyclic adenosine monophosphate (cAMP) is increasingly recognized as having many different roles in plant responses to environmental stimuli. To gain further insights into these roles, Arabidopsis thaliana cell suspension culture was treated with 100 nM of cell permeant 8-bromo-cAMP for 5 or 10 min. Here, applying mass spectrometry and comparative proteomics, 20 proteins were identified as differentially expressed and we noted a specific bias in proteins with a role in abiotic stress, particularly cold and salinity, biotic stress as well as proteins with a role in glycolysis. These findings suggest that cAMP is sufficient to elicit specific stress responses that may in turn induce complex changes to cellular energy homeostasis.

Highlights

  • Environmental factors such as biotic and abiotic stresses can cause constraints on the growth, development and productivity of plants

  • Cyclic nucleotides and 3’,5’-cyclic adenosine monophosphate in particular have long been established as important messengers in prokaryotes as well as in lower and higher eukaryotes [1]

  • The levels of cyclic adenosine monophosphate (cAMP) have been shown to increase in response to biotic stress and subsequently influence calcium (Ca2+) influx by targeting membrane cyclic nucleotide-gated channels (CNGCs) [6], thereby increasing cytosolic free Ca2+

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Summary

Introduction

Environmental factors such as biotic and abiotic stresses can cause constraints on the growth, development and productivity of plants. These stresses disturb cellular homeostasis, and a rapid response is initiated to alleviate the impact of stress. CAMP has been reported to have direct and/or indirect roles in many developmental processes including pollen growth [2] and response to biotic stress [3,4,5]. The levels of cAMP have been shown to increase in response to biotic stress and subsequently influence calcium (Ca2+) influx by targeting membrane cyclic nucleotide-gated channels (CNGCs) [6], thereby increasing cytosolic free Ca2+. When adenylyl cyclase (AC) is activated by the Gα-subunit of recetphteorGb-pasroetdeionnctohuepalendimreaclespytostrem(G.PWCRh)e, nitadcaetnalyylzyelscythcelasfoer(mAaCti)onis oafctcivAaMtePd. bCyyctlhice GAαM-Psutbhuennit of the Gac-tpivroatteesinmcaonuyplseudbsrtercaetepstoarn(dGkPiCnaRs)e,sitscuacthalayszepsrottheeinfokrimnaasteioAn o(PfKcAAM) wP.hCicyhcwlicilAl rMegPultahteenmaacntiyvates manbyioslougbisctarlatpersocaensdsesk.inCayscelsicsuncuhcleaostipdreo-gteatiendkicnhaasneneAl ((PCKNAGC) )w; hsioclhubwleilal dreengyullyaltecymclaansey b(siAoClo)g; ical procpehssoesps.hCodyicelsitcenrauscele(oPtDidEe);-gcaAteMdPchreasnpnoenls(eCeNleGmCe)n;ts-obilnudbilnegad(CenRyElBy)l; cCyRclEaBse-b(isnAdCin)g; pphroostepihno(dCiBesPt)e;rase (PDEca);taclAytMicPsurbeuspnoitnosfePeKleAm(eCn);t-rbeignudlaintogry(CsRubEuBn);itCoRf EPBK-Abi(nRd).ing protein (CBP); catalytic subunit of PKA (C); regulatory subunit of PKA (R)

Results and Discussion
Plant Material and Growth Conditions
Computational Analysis of Functional Enrichment
Conclusions

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