Characterization of the novel interaction between nNos and Caludin-3
Abstract
Neuronal Nitric Oxide Synthase (nNOS) differs from the inducible (iNOS) and endothelial (eNOS) isoforms in a PDZ domain involved in subcellular targeting located at its N-terminus that displays a hydrophobic binding groove that accommodates the C-termini of various cellular proteins. The specific polypeptides involved in these interactions remain mostly undiscovered so we are particularly interested in deciphering new PDZ ligands. By means of in vitro binding techniques and confocal microscopy we have characterized the novel interaction between the PDZ domain of nNOS and Claudin-3, a tight-junction tetraspan membrane protein essential in the paracelullar barrier. Finally, we have proposed tyrosine phosphorylation as one of the possible binding regulation mechanisms.
Downloads
Article download
Crossmark
License
In order to support the global exchange of knowledge, the journal Revista Complutense de Ciencias Veterinarias is allowing unrestricted access to its content as from its publication in this electronic edition, and as such it is an open-access journal. The originals published in this journal are the property of the Complutense University of Madrid and any reproduction thereof in full or in part must cite the source. All content is distributed under a Creative Commons Attribution 4.0 use and distribution licence (CC BY 4.0). This circumstance must be expressly stated in these terms where necessary. You can view the summary and the complete legal text of the licence.
Revista Complutense de Ciencias Veterinarias is an open access journal that does not charge authors for article processing (submission, review or editing) or publication.
