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

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    Type
    Article
    Authors
    Thomas, Ludivine
    Marondedze, Claudius cc
    Ederli, Luisa
    Pasqualini, Stefania
    Gehring, Christoph A cc
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Core Lab
    Bioscience Program
    Core Labs
    Molecular Signalling Group
    Date
    2013-05
    Permanent link to this record
    http://hdl.handle.net/10754/562746
    
    Metadata
    Show full item record
    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.
    Citation
    Thomas, L., Marondedze, C., Ederli, L., Pasqualini, S., & Gehring, C. (2013). Proteomic signatures implicate cAMP in light and temperature responses in Arabidopsis thaliana. Journal of Proteomics, 83, 47–59. doi:10.1016/j.jprot.2013.02.032
    Publisher
    Elsevier BV
    Journal
    Journal of Proteomics
    DOI
    10.1016/j.jprot.2013.02.032
    PubMed ID
    23517717
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.jprot.2013.02.032
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program; Bioscience Core Lab

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