{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T15:03:00Z","timestamp":1790694180244,"version":"4.1.0"},"reference-count":158,"publisher":"MDPI AG","issue":"3","license":[{"start":{"date-parts":[[2022,2,3]],"date-time":"2022-02-03T00:00:00Z","timestamp":1643846400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The FK506-binding protein 52 (FKBP52) belongs to a large family of ubiquitously expressed and highly conserved proteins (FKBPs) that share an FKBP domain and possess Peptidyl-Prolyl Isomerase (PPIase) activity. PPIase activity catalyzes the isomerization of Peptidyl-Prolyl bonds and therefore influences target protein folding and function. FKBP52 is particularly abundant in the nervous system and is partially associated with the microtubule network in different cell types suggesting its implication in microtubule function. Various studies have focused on FKBP52, highlighting its importance in several neuronal microtubule-dependent signaling pathways and its possible implication in neurodegenerative diseases such as tauopathies (i.e., Alzheimer disease) and alpha-synucleinopathies (i.e., Parkinson disease). This review summarizes our current understanding of FKBP52 actions in the microtubule environment, its implication in neuronal signaling and function, its interactions with other members of the FKBPs family and its involvement in neurodegenerative disease.<\/jats:p>","DOI":"10.3390\/ijms23031738","type":"journal-article","created":{"date-parts":[[2022,2,4]],"date-time":"2022-02-04T11:35:17Z","timestamp":1643974517000},"page":"1738","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":18,"title":["FKBP52 in Neuronal Signaling and Neurodegenerative Diseases: A Microtubule Story"],"prefix":"10.3390","volume":"23","author":[{"given":"B\u00e9atrice","family":"Chambraud","sequence":"first","affiliation":[{"name":"INSERM U1195, Universit\u00e9 Paris-Saclay, 80 Rue du G\u00e9n\u00e9ral Leclerc, 94276 Kremlin-Bic\u00eatre, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cillian","family":"Byrne","sequence":"additional","affiliation":[{"name":"Institut Professeur Baulieu, 80 Rue du G\u00e9n\u00e9ral Leclerc, 94276 Kremlin-Bic\u00eatre, France"},{"name":"Laboratoire des Biomol\u00e9cules, LBM7203, CNRS, \u00c9cole Normale Sup\u00e9rieure, PSL University, Sorbonne Universit\u00e9, 75005 Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Geri","family":"Meduri","sequence":"additional","affiliation":[{"name":"Institut Professeur Baulieu, 80 Rue du G\u00e9n\u00e9ral Leclerc, 94276 Kremlin-Bic\u00eatre, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-2532-5085","authenticated-orcid":false,"given":"Etienne Emile","family":"Baulieu","sequence":"additional","affiliation":[{"name":"INSERM U1195, Universit\u00e9 Paris-Saclay, 80 Rue du G\u00e9n\u00e9ral Leclerc, 94276 Kremlin-Bic\u00eatre, France"},{"name":"Institut Professeur Baulieu, 80 Rue du G\u00e9n\u00e9ral Leclerc, 94276 Kremlin-Bic\u00eatre, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-0373-5857","authenticated-orcid":false,"given":"Julien","family":"Giustiniani","sequence":"additional","affiliation":[{"name":"INSERM U1195, Universit\u00e9 Paris-Saclay, 80 Rue du G\u00e9n\u00e9ral Leclerc, 94276 Kremlin-Bic\u00eatre, France"},{"name":"Institut Professeur Baulieu, 80 Rue du G\u00e9n\u00e9ral Leclerc, 94276 Kremlin-Bic\u00eatre, France"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2022,2,3]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1016\/S0959-440X(99)00046-9","article-title":"Enzymes that catalyse the restructuring of proteins","volume":"10","author":"Schiene","year":"2000","journal-title":"Curr. 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