A conserved mechanism for extracellular signaling in eukaryotes and prokaryotes

Marco Gallio*, Gwen Sturgill, Philip Rather, Per Kylsten

*Corresponding author for this work

Research output: Contribution to journalArticle

97 Scopus citations

Abstract

Epidermal growth factor receptor (EGFr) is a key mediator of cell communication during animal development and homeostasis. In Drosophila, the signaling event is commonly regulated by the polytopic membrane protein Rhomboid (RHO), which mediates the proteolytic activation of EGFr ligands, allowing the secretion of the active signal. Until very recently, the biochemical function of RHO had remained elusive. It is now believed that Drosophila RHO is the founder member of a previously undescribed family of serine proteases, and that it could be directly responsible for the unusual, intramembranous cleavage of EGFr ligands. Here we show that the function of RHO is conserved in Gram-negative bacteria. AarA, a Providencia stuartii RHO-related protein, is active in Drosophila on the fly EGFr ligands. Vice versa, Drosophila RHO-1 can effectively rescue the bacterium's ability to produce or release the signal that activates density-dependent gene regulation (or quorum sensing). This study provides the first evidence that prokaryotic and eukaryotic RHOs could have a conserved role in cell communication and that their biochemical properties could be more similar than previously anticipated.

Original languageEnglish (US)
Pages (from-to)12208-12213
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume99
Issue number19
DOIs
StatePublished - Sep 17 2002

ASJC Scopus subject areas

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