Disulfide relays and phosphorylative cascades: partners in redox-mediated signaling pathways View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2005-12

AUTHORS

G Filomeni, G Rotilio, M R Ciriolo

ABSTRACT

Modifications of specific amino-acid residues of proteins are fundamental in order to modulate different signaling processes among which the cascade of phosphorylation represents the most effective example. Recently, also, the modification of the redox state of cysteine residues of certain proteins, which is a widespread mechanism in the regulation of protein function, has been proposed to be involved in signaling pathways. Growing evidence shows that some transcription factors could be modulated by both oxidation and phosphorylation. In particular, the pathways regulated by the mitogen activated protein (MAP) kinases represent well-established examples of the cross talk between redox-mediated signaling and phosphorylative cascades. This review will compare the two modes of signal transduction and propose an evolutionary model of a partnership of the two mechanisms in the eukaryotic cell, with redox-mediated signals being more specific and ancestral and phosphorylative signals being more diffuse but predominant in signal propagation. More... »

PAGES

4401754

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/sj.cdd.4401754

DOI

http://dx.doi.org/10.1038/sj.cdd.4401754

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1031918545

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/16151458


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