000135935 001__ 135935
000135935 005__ 20240627150549.0
000135935 0247_ $$2doi$$a10.3390/biom14050561
000135935 0248_ $$2sideral$$a138948
000135935 037__ $$aART-2024-138948
000135935 041__ $$aeng
000135935 100__ $$aAraujo-Abad, Salome
000135935 245__ $$aUnveiling the Binding between the Armadillo-Repeat Domain of Plakophilin 1 and the Intrinsically Disordered Transcriptional Repressor RYBP
000135935 260__ $$c2024
000135935 5060_ $$aAccess copy available to the general public$$fUnrestricted
000135935 5203_ $$aPlakophilin 1 (PKP1), a member of the p120ctn subfamily of the armadillo (ARM)-repeat-containing proteins, is an important structural component of cell–cell adhesion scaffolds although it can also be ubiquitously found in the cytoplasm and the nucleus. RYBP (RING 1A and YY1 binding protein) is a multifunctional intrinsically disordered protein (IDP) best described as a transcriptional regulator. Both proteins are involved in the development and metastasis of several types of tumors. We studied the binding of the armadillo domain of PKP1 (ARM-PKP1) with RYBP by using in cellulo methods, namely immunofluorescence (IF) and proximity ligation assay (PLA), and in vitro biophysical techniques, namely fluorescence, far-ultraviolet (far-UV) circular dichroism (CD), and isothermal titration calorimetry (ITC). We also characterized the binding of the two proteins by using in silico experiments. Our results showed that there was binding in tumor and non-tumoral cell lines. Binding in vitro between the two proteins was also monitored and found to occur with a dissociation constant in the low micromolar range (~10 μM). Finally, in silico experiments provided additional information on the possible structure of the binding complex, especially on the binding ARM-PKP1 hot-spot. Our findings suggest that RYBP might be a rescuer of the high expression of PKP1 in tumors, where it could decrease the epithelial–mesenchymal transition in some cancer cells.
000135935 536__ $$9info:eu-repo/grantAgreement/ES/DGA/B25-20R$$9info:eu-repo/grantAgreement/ES/DGA/E45-20R$$9info:eu-repo/grantAgreement/ES/ISCIII-ERDF-ESF/PI21-00394$$9info:eu-repo/grantAgreement/ES/MICINN/AEI/PID2021-127296OB-I00
000135935 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000135935 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000135935 700__ $$aRizzuti, Bruno
000135935 700__ $$aVidal, Miguel
000135935 700__ $$0(orcid)0000-0001-5664-1729$$aAbian, Olga$$uUniversidad de Zaragoza
000135935 700__ $$aFárez-Vidal, María Esther
000135935 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, Adrián$$uUniversidad de Zaragoza
000135935 700__ $$aDe Juan Romero, Camino
000135935 700__ $$aNeira, José L.
000135935 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000135935 773__ $$g14, 5 (2024), 561 [17 pp.]$$tBiomolecules$$x2218-273X
000135935 8564_ $$s1921680$$uhttps://zaguan.unizar.es/record/135935/files/texto_completo.pdf$$yVersión publicada
000135935 8564_ $$s2542621$$uhttps://zaguan.unizar.es/record/135935/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000135935 909CO $$ooai:zaguan.unizar.es:135935$$particulos$$pdriver
000135935 951__ $$a2024-06-27-13:20:56
000135935 980__ $$aARTICLE