{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T06:08:53Z","timestamp":1791353333478,"version":"4.3.1"},"reference-count":34,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2015,7,1]]},"abstract":"<jats:p>Phosphatase and tensin homologue (PTEN) and microtubule-associated serine threonine kinase 2 (MAST2) are key negative regulators of survival pathways in neuronal cells. The two proteins interact via the PDZ (PSD-95, Dlg1, Zo-1) domain of MAST2 (MAST2\u2013PDZ). During infection by rabies virus, the viral glycoprotein competes with PTEN for interaction with MAST2\u2013PDZ and promotes neuronal survival. The C-terminal PDZ-binding motifs (PBMs) of the two proteins bind similarly to MAST2\u2013PDZ through an unconventional network of connectivity involving two anchor points. Combining stopped-flow fluorescence, analytical ultracentrifugation (AUC), microcalorimetry and NMR, we document the kinetics of interaction between endogenous and viral ligands to MAST2\u2013PDZ as well as the dynamic and structural effects of these interactions. Viral and PTEN peptide interactions to MAST2\u2013PDZ occur via a unique kinetic step which involves both canonical C-terminal PBM binding and N-terminal anchoring. Indirect effects induced by the PBM binding include modifications to the structure and dynamics of the PDZ dimerization surface which prevent MAST2\u2013PDZ auto-association. Such an energetic communication between binding sites and distal surfaces in PDZ domains provides interesting clues for protein regulation overall.<\/jats:p>","DOI":"10.1042\/bj20141198","type":"journal-article","created":{"date-parts":[[2015,5,6]],"date-time":"2015-05-06T15:45:32Z","timestamp":1430927132000},"page":"159-168","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":22,"title":["Deciphering the unconventional peptide binding to the PDZ domain of MAST2"],"prefix":"10.1042","volume":"469","author":[{"given":"Florent","family":"Delhommel","sequence":"first","affiliation":[{"name":"D\u00e9partement de Biologie Structurale et Chimie, Unit\u00e9 de R\u00e9sonance Magn\u00e9tique Nucl\u00e9aire des Biomol\u00e9cules, Institut Pasteur, F-75724 Paris, France"},{"name":"UMR 3528, CNRS, F-75724 Paris, France"},{"name":"Universit\u00e9 Pierre et Marie Curie, Cellule Pasteur UPMC, rue du Docteur Roux, 75015 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alain","family":"Chaffotte","sequence":"additional","affiliation":[{"name":"D\u00e9partement de Biologie Structurale et Chimie, Unit\u00e9 de R\u00e9sonance Magn\u00e9tique Nucl\u00e9aire des Biomol\u00e9cules, Institut Pasteur, F-75724 Paris, France"},{"name":"UMR 3528, CNRS, F-75724 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Elouan","family":"Terrien","sequence":"additional","affiliation":[{"name":"D\u00e9partement de Biologie Structurale et Chimie, Unit\u00e9 de R\u00e9sonance Magn\u00e9tique Nucl\u00e9aire des Biomol\u00e9cules, Institut Pasteur, F-75724 Paris, France"},{"name":"UMR 3528, CNRS, F-75724 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bertrand","family":"Raynal","sequence":"additional","affiliation":[{"name":"Plate-Forme de Biophysique des Macromol\u00e9cules, Institut Pasteur, F-75724 Paris, France"},{"name":"UMR 3528, CNRS, F-75724 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Henri","family":"Buc","sequence":"additional","affiliation":[{"name":"Invited Scientist, Institut Pasteur F-75724 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Muriel","family":"Delepierre","sequence":"additional","affiliation":[{"name":"D\u00e9partement de Biologie Structurale et Chimie, Unit\u00e9 de R\u00e9sonance Magn\u00e9tique Nucl\u00e9aire des Biomol\u00e9cules, Institut Pasteur, F-75724 Paris, France"},{"name":"UMR 3528, CNRS, F-75724 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florence","family":"Cordier","sequence":"additional","affiliation":[{"name":"D\u00e9partement de Biologie Structurale et Chimie, Unit\u00e9 de R\u00e9sonance Magn\u00e9tique Nucl\u00e9aire des Biomol\u00e9cules, Institut Pasteur, F-75724 Paris, France"},{"name":"UMR 3528, CNRS, F-75724 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicolas","family":"Wolff","sequence":"additional","affiliation":[{"name":"D\u00e9partement de Biologie Structurale et Chimie, Unit\u00e9 de R\u00e9sonance Magn\u00e9tique Nucl\u00e9aire des Biomol\u00e9cules, Institut Pasteur, F-75724 Paris, France"},{"name":"UMR 3528, CNRS, F-75724 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2015,6,19]]},"reference":[{"key":"2021112216202610900_B1","doi-asserted-by":"publisher","first-page":"283","DOI":"10.1038\/sj.cdd.4402258","article-title":"Identification of new kinase clusters required for neurite outgrowth and retraction by a loss-of-function RNA interference screen","volume":"15","author":"Loh","year":"2008","journal-title":"Cell Death Differ."},{"key":"2021112216202610900_B2","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1126\/scisignal.2002941","article-title":"Interference with the PTEN-MAST2 interaction by a viral protein leads to cellular relocalization of PTEN","volume":"5","author":"Terrien","year":"2012","journal-title":"Sci. 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