Transmembrane signal transduction is a feature common to all eukaryotic and prokaryotic cells. We now understand that a subset of the signalling mechanisms used by eukaryotes and prokaryotes are not just similar in principle, but actually use homologous proteins. These are the histidine-aspartate phosphorelays, signalling systems of eubacterial origin, now known to be widespread in eukaryotes outside the animal kingdom. Genome projects are revealing that His-Asp phosphorelays are present as multigene families in lower eukaryotes and in plants. A major challenge is to understand how these ‘novel’ signal transduction systems form integrated networks with the more familiar signalling mechanisms also present in eukaryotic cells. Already, phosphorelays have been characterised that regulate MAP kinase cascades and the cAMP/PKA pathway. The probable absence of His-Asp phosphorelays from animals has generated interest in their potential as targets for anti-microbial therapy, including antifungals. Recent findings suggest that this approach holds promise.
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JOURNAL ARTICLE| 15 September 2000
Eukaryotic signal transduction via histidine-aspartate phosphorelay
Online Issn: 1477-9137
Print Issn: 0021-9533
© 2000 by Company of Biologists
J Cell Sci (2000) 113 (18): 3141–3150.
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P. Thomason, R. Kay; Eukaryotic signal transduction via histidine-aspartate phosphorelay. J Cell Sci 15 September 2000; 113 (18): 3141–3150. doi: https://doi.org/10.1242/jcs.113.18.3141
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