000150688 001__ 150688
000150688 005__ 20251017144641.0
000150688 0247_ $$2doi$$a10.1002/advs.202415566
000150688 0248_ $$2sideral$$a142794
000150688 037__ $$aART-2025-142794
000150688 041__ $$aeng
000150688 100__ $$aBaños-Jaime, Blanca
000150688 245__ $$aEvolutionary Pro-To-Thr Mutation in the Intrinsically Disordered Domain of ANP32 Family Members Modulates Their Target Binding Modes
000150688 260__ $$c2025
000150688 5060_ $$aAccess copy available to the general public$$fUnrestricted
000150688 5203_ $$aGene duplication has allowed protein evolution toward novel functions and mechanisms. The differences between paralogous genes frequently rely on the sequence of disordered regions. For instance, in mammals, the chaperones ANP32A and ANP32B share a common evolutionary line and have some exchangeable functions based on their similar N‐terminal domains. Nevertheless, their C‐terminal low‐complexity‐acidic‐regions (LCARs) display substantial sequence differences, unveiling some degree of variability between them, in agreement with their different tissue‐specific expression patterns. These structural and computational results indicate that a substitution in the vicinity of the nuclear localization signal (NLS), of Pro in ANP32A for Thr in ANP32B, determines the overall compactness of the C‐terminal LCAR. The different structural properties of the disordered region affect the binding mode of ANP32 members to their targets. This type of divergent binding mode is exemplified with the extra‐mitochondrial cytochrome c (Cc), a well‐known ANP32B partner and which now determine also binds to ANP32A; and with the RNA binding protein HuR, whose export to the cytoplasm is mediated by ANP32 proteins under stress. Therefore, differential expression patterns of ANP32A or ANP32B may affect the regulation of Cc and HuR and can help to explain the distinct roles of these proteins in diseases.
000150688 536__ $$9info:eu-repo/grantAgreement/ES/MECD/FPU13-04373$$9info:eu-repo/grantAgreement/ES/MECD/FPU16-01513$$9info:eu-repo/grantAgreement/ES/MECD/FPU18-06577$$9info:eu-repo/grantAgreement/ES/MICINN/PID2021-126663NB-I00
000150688 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttps://creativecommons.org/licenses/by/4.0/deed.es
000150688 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000150688 700__ $$aUceda-Mayo, Ana B.
000150688 700__ $$aRivero-Rodríguez, Francisco
000150688 700__ $$aCasado-Combreras, Miguel Á.
000150688 700__ $$aVelázquez-Cruz, Alejandro
000150688 700__ $$0(orcid)0000-0001-5702-4538$$aVelázquez-Campoy, Adrián$$uUniversidad de Zaragoza
000150688 700__ $$aCorrales-Guerrero, Laura
000150688 700__ $$aDe la Rosa, Miguel A.
000150688 700__ $$aDíaz-Moreno, Irene
000150688 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000150688 773__ $$g12, 12 (2025), 2415566 [14 pp.]$$pAdv. sci.$$tAdvanced Science$$x2198-3844
000150688 8564_ $$s7423527$$uhttps://zaguan.unizar.es/record/150688/files/texto_completo.pdf$$yVersión publicada
000150688 8564_ $$s2607546$$uhttps://zaguan.unizar.es/record/150688/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000150688 909CO $$ooai:zaguan.unizar.es:150688$$particulos$$pdriver
000150688 951__ $$a2025-10-17-14:31:49
000150688 980__ $$aARTICLE