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dc.creatorPeris-Martínez, I. (Irene)-
dc.creatorRomero-Murillo, S. (Silvia)-
dc.creatorVicente, C. (Carmen)-
dc.creatorNarla, G. (Goutham)-
dc.creatorOdero, M.D. (Maria Dolores)-
dc.date.accessioned2023-09-20T11:09:40Z-
dc.date.available2023-09-20T11:09:40Z-
dc.date.issued2023-
dc.identifier.citationPeris-Martínez, I. (Irene); Romero-Murillo, S. (Silvia); Vicente, C. (Carmen); et al. "Regulation and role of the PP2A-B56 holoenzyme family in cancer". Biochimica et Biophysica Acta (BBA) - Reviews on Cancer Supports open access. 1878, 2023, 188953es_ES
dc.identifier.issn0304-419X-
dc.identifier.urihttps://hdl.handle.net/10171/67257-
dc.description.abstractProtein phosphatase 2A (PP2A) inactivation is common in cancer, leading to sustained activation of pro-survival and growth-promoting pathways. PP2A consists of a scaffolding A-subunit, a catalytic C-subunit, and a regulatory B-subunit. The functional complexity of PP2A holoenzymes arises mainly through the vast repertoire of regulatory B-subunits, which determine both their substrate specificity and their subcellular localization. Therefore, a major challenge for developing more effective therapeutic strategies for cancer is to identify the specific PP2A complexes to be targeted. Of note, the development of small molecules specifically directed at PP2A-B56α has opened new therapeutic avenues in both solid and hematological tumors. Here, we focus on the B56/PR61 family of PP2A regulatory subunits, which have a central role in directing PP2A tumor suppressor activity. We provide an overview of the mechanisms controlling the formation and regulation of these complexes, the pathways they control, and the mechanisms underlying their deregulation in cancer.es_ES
dc.description.sponsorshipThis work was supported by grants from Instituto de Salud Carlos III (FIS) – Acción Estratégica en Salud (PI20/01558, M.D.O.) and CIBERONC (CB16/12/00489, M.D.O.), co-financed with FEDER funds. NIH/NCI grants (R01 CA-181654 and R01 CA-240993, G.N.). I.P. has received funding from “La Caixa” Banking Foundation and Asociación de Amigos (University of Navarra). S.R-M. is supported by a grant from the Fundación para la Investigación Médica Aplicada (AC FIMA) and from Gobierno de Navarra (344E/2023). C.V. is supported by a grant from the Spanish Association Against Cancer (Fundación Científica AECC, INVES18061ODER).es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.relationinfo_eu-repo/grantAgreement/MINECO/Ayudas a la incorporación de nuevas áreas temáticas y nuevos grupos al Consorcio CIBER (AE de Salud 2016)/CB16/12/00489/[ES]/CANCERes_ES
dc.rightsinfo:eu-repo/semantics/openAccesses_ES
dc.subjectPhosphatasees_ES
dc.subjectPP2Aes_ES
dc.subjectB56/PR61es_ES
dc.subjectCanceres_ES
dc.subjectPP2A-activatorses_ES
dc.subjectSMAPes_ES
dc.subjectTumor suppressores_ES
dc.subjectSLiMes_ES
dc.titleRegulation and role of the PP2A-B56 holoenzyme family in canceres_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.description.noteThis is an open access article under the CC BY-NC-ND licensees_ES
dc.identifier.doi10.1016/j.bbcan.2023.188953-
dadun.citation.publicationNameBBA - Reviews on Canceres_ES
dadun.citation.startingPage188953es_ES
dadun.citation.volume1878es_ES
dc.identifier.pmid37437699-

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