hCEACAM1-4L downregulates hDAF-associated signalling after being recognized by the Dr adhesin of diffusely adhering Escherichia coli

Rougeaux, Clémence, Berger, Cédric N. ORCID: https://orcid.org/0000-0002-1316-5985 and Servin, Alain L. 2008. hCEACAM1-4L downregulates hDAF-associated signalling after being recognized by the Dr adhesin of diffusely adhering Escherichia coli. Cellular Microbiology 10 (3) , pp. 632-654. 10.1111/j.1462-5822.2007.01072.x

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Abstract

Human decay accelerating factor (hDAF, CD55) and members of the carcinoembryonic‐antigen‐related cell‐adhesion molecules (hCEACAMs) family are recognized as receptors by Gram‐negative, diffusely adhering Escherichia coli (DAEC) strains expressing Afa/Dr adhesins. We report here that hCEACAM1‐4L has a key function in downregulating the protein tyrosine Src kinase associated with hDAF signalling. After infecting HeLa epithelial cells stably transfected with hCEACAM1‐4L cDNA with Dr adhesin‐positive E. coli, the amount of the pTyr416‐active form of the Src protein decreased, whereas that of the pTyr527‐inactive form of Src protein did not increase. This downregulation of the Src protein implies that part of the hCEACAM1‐4L protein had been translocated into lipid rafts, the protein was phosphorylated at Tyr residues in the cytoplasmic domain, and it was physically associated with the protein tyrosine phosphatase, SHP‐2. Finally, we found that the hCEACAM1‐4L‐associated SHP‐2 was not phosphorylated and lacked phosphatase activity, suggesting that the downregulation of Src protein associated with hDAF signalling results from the absence of dephosphorylation of the pTyr527‐inactive form necessary for Src kinase activation.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Publisher:	Wiley: 12 months
ISSN:	1462-5814
Date of Acceptance:	27 September 2007
Last Modified:	24 Oct 2022 07:21
URI:	https://orca.cardiff.ac.uk/id/eprint/114727

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