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Disordered proteins with nucleic acidbinding ability drive the formation of reversible micron\u2010sized condensates capable of controlling nucleic acid processing\/transport. This mechanism, achieved via liquid\u2013liquid phase separation (LLPS), underlies the formation of long\u2010studied membraneless organelles (e.g., nucleolus) and various transient condensates formed by driver proteins. The prion protein (PrP) is not a classical nucleic acid\u2010binding protein. However, it binds nucleic acids with high affinity, undergoes nucleocytoplasmic shuttling, contains a long intrinsically disordered region rich in glycines and evenly spaced aromatic residues, among other biochemical\/biophysical properties of bona fide drivers of phase transitions. Because of this, our group and others have characterized LLPS of recombinant PrP. In vitro phase separation of PrP is modulated by nucleic acid aptamers, and depending on the aptamer conformation, the liquid droplets evolve to solid\u2010like species. Herein, we discuss recent studies and previous evidence supporting PrP phase transitions. We focus on the central role of LLPS related to PrP physiology and pathology, with a special emphasis on the interaction of PrP with different ligands, such as proteins and nucleic acids, which can play a role in prion disease pathogenesis. Finally, we comment on therapeutic strategies directed at the non\u2010functional phase separation that could potentially tackle prion diseases or other protein misfolding disorders.<jats:boxed-text content-type=\"graphic\" position=\"anchor\"><jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc15586-fig-0004-m.png\"><jats:alt-text>image<\/jats:alt-text><\/jats:graphic><\/jats:boxed-text><\/jats:p>","DOI":"10.1111\/jnc.15586","type":"journal-article","created":{"date-parts":[[2022,2,12]],"date-time":"2022-02-12T06:28:56Z","timestamp":1644647336000},"page":"58-75","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["Phase separation of the mammalian prion protein: Physiological and pathological perspectives"],"prefix":"10.1111","volume":"166","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-1247-2606","authenticated-orcid":false,"given":"Mariana J.","family":"do Amaral","sequence":"first","affiliation":[{"name":"Faculty of Pharmacy Universidade Federal do Rio de Janeiro  Rio de Janeiro\u2010RJ Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-1956-1433","authenticated-orcid":false,"given":"Maria Heloisa O.","family":"Freire","sequence":"additional","affiliation":[{"name":"Faculty of Pharmacy Universidade Federal do Rio de Janeiro  Rio de Janeiro\u2010RJ Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4921-8185","authenticated-orcid":false,"given":"Marcius S.","family":"Almeida","sequence":"additional","affiliation":[{"name":"Medical Biochemistry Institute, Protein Advanced Biochemistry, National Center for Structural Biology and Bioimaging Universidade Federal do Rio de Janeiro  Rio de Janeiro\u2010RJ Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-5118-6931","authenticated-orcid":false,"given":"Anderson S.","family":"Pinheiro","sequence":"additional","affiliation":[{"name":"Department of Biochemistry, Institute of Chemistry Universidade Federal do Rio de Janeiro  Rio de Janeiro\u2010RJ Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-4278-212X","authenticated-orcid":false,"given":"Yraima","family":"Cordeiro","sequence":"additional","affiliation":[{"name":"Faculty of Pharmacy Universidade Federal do Rio de Janeiro  Rio de Janeiro\u2010RJ Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2022,3,5]]},"reference":[{"key":"e_1_2_14_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.febslet.2010.04.040"},{"key":"e_1_2_14_3_1","article-title":"Spatiotemporal modulations in heterotypic condensates of prion and \u03b1\u2010synuclein control phase transitions and amyloid conversion","author":"Agarwal A.","year":"2021","journal-title":"bioRxiv"},{"key":"e_1_2_14_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2021.167368"},{"key":"e_1_2_14_5_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.2100968118"},{"key":"e_1_2_14_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2009.05.041"},{"key":"e_1_2_14_7_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41594-018-0084-y"},{"key":"e_1_2_14_8_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2018.12.035"},{"key":"e_1_2_14_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2009.02.044"},{"key":"e_1_2_14_10_1","doi-asserted-by":"publisher","DOI":"10.1002\/bies.201600042"},{"key":"e_1_2_14_11_1","doi-asserted-by":"publisher","DOI":"10.1038\/s41580-020-00326-6"},{"key":"e_1_2_14_12_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1922365117"},{"key":"e_1_2_14_13_1","doi-asserted-by":"crossref","unstructured":"Amaral M. 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