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Article ; Online: FKBP52 in Neuronal Signaling and Neurodegenerative Diseases: A Microtubule Story.

Chambraud, Béatrice / Byrne, Cillian / Meduri, Geri / Baulieu, Etienne Emile / Giustiniani, Julien

International journal of molecular sciences

2022 Volume 23, Issue 3

Abstract: 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 ...

Abstract	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.
MeSH term(s)	Animals ; Humans ; Microtubules/metabolism ; Neurodegenerative Diseases/metabolism ; Neurons/metabolism ; Protein Aggregates ; Signal Transduction ; Tacrolimus Binding Proteins/metabolism
Chemical Substances	Protein Aggregates ; Tacrolimus Binding Proteins (EC 5.2.1.-) ; tacrolimus binding protein 4 (EC 5.2.1.-)
Language	English
Publishing date	2022-02-03
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms23031738
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Article ; Online: Concomitant Neuronal Tau Deposition and FKBP52 Decrease Is an Early Feature of Different Human and Experimental Tauopathies.

Meduri, Geri / Guillemeau, Kevin / Daguinot, Corentin / Dounane, Omar / Genet, Melanie / Ferrara, Luigi / Chambraud, Beatrice / Baulieu, Etienne Emile / Giustiniani, Julien

Journal of Alzheimer's disease : JAD

2023 Volume 94, Issue 1, Page(s) 313–331

Abstract: Background: Pathological tau proteins constitute neurofibrillary tangles that accumulate in tauopathies including Alzheimer's disease (AD), progressive supranuclear palsy (PSP), and familial frontotemporal lobar degeneration (FTLD-Tau). We previously ... ...

Abstract	Background: Pathological tau proteins constitute neurofibrillary tangles that accumulate in tauopathies including Alzheimer's disease (AD), progressive supranuclear palsy (PSP), and familial frontotemporal lobar degeneration (FTLD-Tau). We previously showed that the FKBP52 immunophilin interacts functionally with tau and strongly decreases in AD brain neurons in correlation with tau deposition. We also reported that FKBP52 co-localizes with autophagy-lysosomal markers and an early pathological tau isoform in AD neurons, suggesting its involvement in autophagic tau clearance. Objective: Our objective was to evaluate if differences in neuronal FKBP52 expression levels and subcellular localization might be detected in AD, PSP, familial FTLD-Tau, and in the hTau-P301 S mouse model compared to controls. Methods: Cell by cell immunohistofluorescence analyses and quantification of FKBP52 were performed on postmortem brain samples of some human tauopathies and on hTau-P301 S mice spinal cords. Results: We describe a similar FKBP52 decrease and its localization with early pathological tau forms in the neuronal autophagy-lysosomal pathway in various tauopathies and hTau-P301 S mice. We find that FKBP52 decreases early during the pathologic process as it occurs in rare neurons with tau deposits in the marginally affected frontal cortex region of AD Braak IV brains and in the spinal cord of symptomless 1-month-old hTau-P301 S mice. Conclusion: As FKBP52 plays a significant role in cellular signaling and conceivably in tau clearance, our data support the idea that the prevention of FKBP52 decrease or the restoration of its normal expression at early pathologic stages might represent a new potential therapeutic approach in tauopathies including AD, familial FTLD-Tau, and PSP.
MeSH term(s)	Humans ; Mice ; Animals ; Tauopathies/pathology ; tau Proteins/metabolism ; Alzheimer Disease/pathology ; Neurons/metabolism ; Frontotemporal Lobar Degeneration/pathology ; Brain/pathology
Chemical Substances	tacrolimus binding protein 4 (EC 5.2.1.-) ; tau Proteins
Language	English
Publishing date	2023-05-29
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/JAD-230127
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Article ; Online: Decrease of neuronal FKBP4/FKBP52 modulates perinuclear lysosomal positioning and MAPT/Tau behavior during MAPT/Tau-induced proteotoxic stress.

Chambraud, Béatrice / Daguinot, Corentin / Guillemeau, Kevin / Genet, Melanie / Dounane, Omar / Meduri, Geri / Poüs, Christian / Baulieu, Etienne Emile / Giustiniani, Julien

Autophagy

2021 Volume 17, Issue 11, Page(s) 3491–3510

Abstract: Defects of autophagy-lysosomal protein degradation are thought to contribute to the pathogenesis of several neurodegenerative diseases, and the accumulation of aggregation prone proteins such as MAPT/Tau in Alzheimer disease (AD). We previously showed ... ...

Abstract	Defects of autophagy-lysosomal protein degradation are thought to contribute to the pathogenesis of several neurodegenerative diseases, and the accumulation of aggregation prone proteins such as MAPT/Tau in Alzheimer disease (AD). We previously showed the localization of the immunophilin FKBP4/FKBP52 in the lysosomal system of healthy human neurons suggesting its possible role in lysosome function. We also showed that decreased FKBP4 levels in AD brain neurons correlate with abnormal MAPT accumulation and aggregation. In this study, we demonstrate that FKBP4 decrease in a human neuronal cell line (SH-SY5Y) and in dorsal root ganglion (DRG) neurons from human MAPT
MeSH term(s)	Aged ; Aged, 80 and over ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Animals ; Autophagy/physiology ; Brain/metabolism ; Brain/pathology ; Cell Line ; Cells, Cultured ; Female ; Humans ; Lysosomes/metabolism ; Male ; Mice ; Mice, Transgenic ; Microtubule-Associated Proteins/metabolism ; Middle Aged ; Models, Neurological ; Neurons/metabolism ; Neurons/pathology ; Sequestosome-1 Protein/metabolism ; Stress, Physiological ; Tacrolimus Binding Proteins/deficiency ; Tacrolimus Binding Proteins/metabolism ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	MAP1LC3A protein, human ; MAPT protein, human ; Microtubule-Associated Proteins ; SQSTM1 protein, human ; Sequestosome-1 Protein ; tau Proteins ; Tacrolimus Binding Proteins (EC 5.2.1.-) ; tacrolimus binding protein 4 (EC 5.2.1.-)
Language	English
Publishing date	2021-01-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2454135-7
ISSN	1554-8635 ; 1554-8627
ISSN (online)	1554-8635
ISSN	1554-8627
DOI	10.1080/15548627.2021.1875611
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Article ; Online: Caspase-cleaved Tau-D(421) is colocalized with the immunophilin FKBP52 in the autophagy-endolysosomal system of Alzheimer's disease neurons.

Meduri, Geri / Guillemeau, Kevin / Dounane, Omar / Sazdovitch, Véronique / Duyckaerts, Charles / Chambraud, Béatrice / Baulieu, Etienne Emile / Giustiniani, Julien

Neurobiology of aging

2016 Volume 46, Page(s) 124–137

Abstract: Pathologic modifications of the Tau protein leading to neurofibrillary tangle (NFT) formation are a common feature of a wide range of neurodegenerative diseases known as tauopathies, which include Alzheimer's disease (AD). We previously showed that the ... ...

Abstract	Pathologic modifications of the Tau protein leading to neurofibrillary tangle (NFT) formation are a common feature of a wide range of neurodegenerative diseases known as tauopathies, which include Alzheimer's disease (AD). We previously showed that the immunophilin FKBP52 physically and functionally interacts with Tau, and we recently reported that FKBP52 levels are abnormally low in AD patients' brains. To decipher the mechanism of FKBP52 decrease in AD brains, we performed multiple labeling immunohistofluorescence and lysosomal purification using postmortem brain samples of healthy controls (n = 8) and AD (n = 20) patients. Confocal analysis revealed that FKBP52 localizes to the endolysosomal system. We also report FKBP52 colocalization with the truncated Tau-D(421) in the autophagy-endolysosomal system in some AD neurons and that the decrease of FKBP52 correlates with NFT formation. Additional experiments of autophagy inhibition in Tau-inducible SH-SY5Y cells allowed demonstrating FKBP52 release in the extracellular milieu. Our findings point out the possibility that FKBP52 could be abnormally released from NFTs negative neurons in AD brains in correlation with the early pathologic Tau-D(421) neuronal accumulation.
MeSH term(s)	Aged ; Aged, 80 and over ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Autophagy ; Brain/metabolism ; Caspases ; Cells, Cultured ; Female ; Humans ; Lysosomes/metabolism ; Male ; Middle Aged ; Neurofibrillary Tangles/metabolism ; Neurofibrillary Tangles/pathology ; Neurons/cytology ; Neurons/metabolism ; Tacrolimus Binding Proteins/metabolism ; Tacrolimus Binding Proteins/physiology ; Tauopathies/genetics ; Tauopathies/metabolism ; tau Proteins/metabolism
Chemical Substances	tau Proteins ; Caspases (EC 3.4.22.-) ; Tacrolimus Binding Proteins (EC 5.2.1.-) ; tacrolimus binding protein 4 (EC 5.2.1.-)
Language	English
Publishing date	2016-10
Publishing country	United States
Document type	Journal Article
ZDB-ID	604505-4
ISSN	1558-1497 ; 0197-4580
ISSN (online)	1558-1497
ISSN	0197-4580
DOI	10.1016/j.neurobiolaging.2016.06.017
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Article ; Online: A β-Turn Motif in the Steroid Hormone Receptor's Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52.

Byrne, Cillian / Henen, Morkos A / Belnou, Mathilde / Cantrelle, François-Xavier / Kamah, Amina / Qi, Haoling / Giustiniani, Julien / Chambraud, Béatrice / Baulieu, Etienne-Emile / Lippens, Guy / Landrieu, Isabelle / Jacquot, Yves

Biochemistry

2016 Volume 55, Issue 38, Page(s) 5366–5376

Abstract: The immunophilin FKBP52 interacts with nuclear steroid hormone receptors. Studying the crystal structure of human estrogen receptor α (hERα) and using nuclear magnetic resonance, we show here that the short V(364)PGF(367) sequence, which is located ... ...

Abstract	The immunophilin FKBP52 interacts with nuclear steroid hormone receptors. Studying the crystal structure of human estrogen receptor α (hERα) and using nuclear magnetic resonance, we show here that the short V(364)PGF(367) sequence, which is located within its ligand-binding domain and adopts a type II β-turn conformation in the protein, binds the peptidyl-prolyl isomerase (PPIase or rotamase) FK1 domain of FKBP52. Interestingly, this turn motif displays strong similarities with the FKBP52 FK1 domain-binding moiety of macrolide immunomodulators such as rapamycin and GPI-1046, an immunophilin ligand with neuroprotective characteristics. An increase in the hydrophobicity of the residue preceding the proline and cyclization of the VPGF peptide strengthen its recognition by the FK1 domain of FKBP52. Replacement of the Pro residue with a dimethylproline also enhances this interaction. Our study not only contributes to a better understanding of how the interaction between the FK1 domain of FKBP52 and steroid hormone receptors most likely works but also opens new avenues for the synthesis of FKBP52 FK1 peptide ligands appropriate for the control of hormone-dependent physiological mechanisms or of the functioning of the Tau protein. Indeed, it has been shown that FKBP52 is involved in the intraneuronal dynamics of the Tau protein.
MeSH term(s)	Binding Sites ; Catalytic Domain ; Ligands ; Nuclear Magnetic Resonance, Biomolecular ; Peptidylprolyl Isomerase/metabolism ; Protein Binding ; Receptors, Cytoplasmic and Nuclear/metabolism ; Steroids/metabolism ; Thermodynamics
Chemical Substances	Ligands ; Receptors, Cytoplasmic and Nuclear ; Steroids ; Peptidylprolyl Isomerase (EC 5.2.1.8)
Language	English
Publishing date	2016-09-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/acs.biochem.6b00506
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Article: A Î²-Turn Motif in the Steroid Hormone Receptorâs Ligand-Binding Domains Interacts with the Peptidyl-prolyl Isomerase (PPIase) Catalytic Site of the Immunophilin FKBP52

Byrne, Cillian / Henen Morkos A / Belnou Mathilde / Cantrelle FrancÌ§ois-Xavier / Kamah Amina / Qi Haoling / Giustiniani Julien / Chambraud BeÌatrice / Baulieu Etienne-Emile / Lippens Guy / Landrieu Isabelle / Jacquot Yves

Biochemistry. 2016 Sept. 27, v. 55, no. 38

2016

Abstract: The immunophilin FKBP52 interacts with nuclear steroid hormone receptors. Studying the crystal structure of human estrogen receptor Î± (hERÎ±) and using nuclear magnetic resonance, we show here that the short VÂ³â¶â´PGFÂ³â¶â· sequence, which is ... ...

Abstract	The immunophilin FKBP52 interacts with nuclear steroid hormone receptors. Studying the crystal structure of human estrogen receptor Î± (hERÎ±) and using nuclear magnetic resonance, we show here that the short VÂ³â¶â´PGFÂ³â¶â· sequence, which is located within its ligand-binding domain and adopts a type II Î²-turn conformation in the protein, binds the peptidyl-prolyl isomerase (PPIase or rotamase) FK1 domain of FKBP52. Interestingly, this turn motif displays strong similarities with the FKBP52 FK1 domain-binding moiety of macrolide immunomodulators such as rapamycin and GPI-1046, an immunophilin ligand with neuroprotective characteristics. An increase in the hydrophobicity of the residue preceding the proline and cyclization of the VPGF peptide strengthen its recognition by the FK1 domain of FKBP52. Replacement of the Pro residue with a dimethylproline also enhances this interaction. Our study not only contributes to a better understanding of how the interaction between the FK1 domain of FKBP52 and steroid hormone receptors most likely works but also opens new avenues for the synthesis of FKBP52 FK1 peptide ligands appropriate for the control of hormone-dependent physiological mechanisms or of the functioning of the Tau protein. Indeed, it has been shown that FKBP52 is involved in the intraneuronal dynamics of the Tau protein.
Keywords	active sites ; crystal structure ; estrogen receptors ; humans ; hydrophobicity ; immunomodulators ; ligands ; macrolides ; nuclear magnetic resonance spectroscopy ; peptidylprolyl isomerase ; proline ; protein conformation ; steroid hormone receptors
Language	English
Dates of publication	2016-0927
Size	p. 5366-5376.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021%2Facs.biochem.6b00506
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Article ; Online: Tubulin acetylation favors Hsp90 recruitment to microtubules and stimulates the signaling function of the Hsp90 clients Akt/PKB and p53.

Giustiniani, Julien / Daire, Vanessa / Cantaloube, Isabelle / Durand, Geneviève / Poüs, Christian / Perdiz, Daniel / Baillet, Anita

Cellular signalling

2009 Volume 21, Issue 4, Page(s) 529–539

Abstract: Involved in a wide range of cellular processes such as signal transduction, microtubules are highly dynamic polymers that accumulate various post-translational modifications including polyglutamylation, polyglycylation, carboxyterminal cleavage and ... ...

Abstract	Involved in a wide range of cellular processes such as signal transduction, microtubules are highly dynamic polymers that accumulate various post-translational modifications including polyglutamylation, polyglycylation, carboxyterminal cleavage and acetylation, the functions of which just begin to be uncovered. The molecular chaperone Hsp90, which is essential for the folding and activity of numerous client proteins involved in cell proliferation and apoptosis, associates with the microtubule network but the effects of tubulin post-translational modifications on its microtubule binding has not yet been investigated. Herein, we show that both the constitutive (beta) and the inducible (alpha) Hsp90 isoforms bind to microtubules in a way that depends on the level of tubulin acetylation. Tubulin acetylation also stimulates the binding and the signaling function of at least two of its client proteins, the kinase Akt/PKB and the transcription factor p53. This study highlights the role of tubulin acetylation in modulating microtubule-based transport of Hsp90-chaperoned proteins and thus in regulating signaling dynamics in the cytoplasm.
MeSH term(s)	Acetylation ; Amino Acid Substitution ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; HeLa Cells ; Humans ; Hydroxamic Acids/pharmacology ; Microtubules/drug effects ; Microtubules/metabolism ; Mutation, Missense ; Neoplasm Proteins/physiology ; Point Mutation ; Protein Processing, Post-Translational ; Protein Transport/physiology ; Proto-Oncogene Proteins c-akt/physiology ; Signal Transduction/drug effects ; Tubulin/genetics ; Tubulin/physiology ; Tumor Suppressor Protein p53/physiology
Chemical Substances	Hydroxamic Acids ; Neoplasm Proteins ; TP53 protein, human ; Tubulin ; Tumor Suppressor Protein p53 ; trichostatin A (3X2S926L3Z) ; AKT1 protein, human (EC 2.7.11.1) ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1)
Language	English
Publishing date	2009-04
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1002702-6
ISSN	1873-3913 ; 0898-6568
ISSN (online)	1873-3913
ISSN	0898-6568
DOI	10.1016/j.cellsig.2008.12.004
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Article ; Online: Decrease of the immunophilin FKBP52 accumulation in human brains of Alzheimer's disease and FTDP-17.

Giustiniani, Julien / Sineus, Marlène / Sardin, Elodie / Dounane, Omar / Panchal, Maï / Sazdovitch, Véronique / Duyckaerts, Charles / Chambraud, Béatrice / Baulieu, Etienne-Emile

Journal of Alzheimer's disease : JAD

2012 Volume 29, Issue 2, Page(s) 471–483

Abstract: Human neurodegenerative diseases characterized by abnormal intraneuronal inclusions of the tau protein, or "tauopathies", include Alzheimer's disease (AD), Pick's disease, progressive supranuclear palsy, corticobasal degeneration as well as fronto- ... ...

Abstract	Human neurodegenerative diseases characterized by abnormal intraneuronal inclusions of the tau protein, or "tauopathies", include Alzheimer's disease (AD), Pick's disease, progressive supranuclear palsy, corticobasal degeneration as well as fronto-temporal dementia and Parkinsonism linked to chromosome 17 (FTDP-17). Several abnormalities of tau may contribute to the pathological processes, yet the mechanisms involved in tau cellular toxicity remain unclear. Previously, we demonstrated an interaction between various isoforms of tau and the immunophilin FKBP52 (FK506-Binding Protein), suggesting a direct involvement of FKBP52 in tau function. Here we analyze the expression of FKBP52 in human brains of patients with different tauopathies, including AD. Immunohistofluorescence studies carried out on cerebral cortex in different tauopathies reveal that FKBP52 is not sequestered by filamentous tau inclusions while FKBP52 is colocalized with tau in the control case brains. We found that FKBP52 expression level is abnormally low in frontal cortex of AD and FTDP-17 brains, as compared to controls, despite no alteration in the FKBP52 mRNA expression level. The possible involvement of FKBP52 in pathological tau expression/function is discussed.
MeSH term(s)	Aged ; Aged, 80 and over ; Alzheimer Disease/genetics ; Alzheimer Disease/metabolism ; Alzheimer Disease/pathology ; Brain/metabolism ; Female ; Frontotemporal Dementia/genetics ; Frontotemporal Dementia/metabolism ; Frontotemporal Dementia/pathology ; Gene Expression Regulation/physiology ; Humans ; Male ; Middle Aged ; Neurofibrillary Tangles/pathology ; RNA, Messenger/metabolism ; Tacrolimus Binding Proteins/genetics ; Tacrolimus Binding Proteins/metabolism ; tau Proteins/genetics ; tau Proteins/metabolism
Chemical Substances	MAPT protein, human ; RNA, Messenger ; tau Proteins ; Tacrolimus Binding Proteins (EC 5.2.1.-) ; tacrolimus binding protein 4 (EC 5.2.1.-)
Language	English
Publishing date	2012
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1440127-7
ISSN	1875-8908 ; 1387-2877
ISSN (online)	1875-8908
ISSN	1387-2877
DOI	10.3233/JAD-2011-111895
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Article: A role for FKBP52 in Tau protein function

Chambraud, BÃ©atrice / Sardin, Elodie / Giustiniani, Julien / Dounane, Omar / Schumacher, Michael / Goedert, Michel / Baulieu, Etienne-Emile

Proceedings of the National Academy of Sciences of the United States of America. 2010 Feb. 9, v. 107, no. 6

2010

Abstract: Tau is a microtubule-associated protein, which is widely expressed in the central nervous system, predominantly in neurons, where it regulates microtubule dynamics, axonal transport, and neurite outgrowth. The aberrant assembly of Tau is the hallmark of ... ...

Abstract	Tau is a microtubule-associated protein, which is widely expressed in the central nervous system, predominantly in neurons, where it regulates microtubule dynamics, axonal transport, and neurite outgrowth. The aberrant assembly of Tau is the hallmark of several human neurodegenerative diseases, collectively known as tauopathies. They include Alzheimer's disease, Pick's disease, progressive supranuclear palsy, and frontotemporal dementia and parkinsonism linked to chromosome 17. Several abnormalities in Tau, such as hyperphosphorylation and aggregation, alter its function and are central to the pathogenic process. Here, we describe biochemical and functional interactions between FKBP52 and Tau. FKBP52 is a member of the FKBP (FK506-binding protein) family that comprises intracellular protein effectors of immunosuppressive drugs (such as FK506 and rapamycin). We found that FKBP52, which is abundant in brain, binds directly and specifically to Tau, especially in its hyperphosphorylated form. The relevance of this observation was confirmed by the colocalization of both proteins in the distal part of the axons of cortical neurons and by the antagonistic effect of FKBP52 on the ability of Tau to promote microtubule assembly. Overexpression of FKBP52 in differentiated PC12 cells prevented the accumulation of Tau and resulted in reduced neurite length. Taken together, these findings indicate a role for FKBP52 in Tau function and may help to decipher and modulate the events involved in Tau-induced neurodegeneration.
Keywords	Alzheimer disease ; Parkinson disease ; axonal transport ; brain ; chromosomes ; drugs ; humans ; microtubules ; neurites ; proteins
Language	English
Dates of publication	2010-0209
Size	p. 2658-2663.
Publishing place	National Academy of Sciences
Document type	Article
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.0914957107
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Article ; Online: The FK506-binding protein FKBP52 in vitro induces aggregation of truncated Tau forms with prion-like behavior.

Giustiniani, Julien / Guillemeau, Kevin / Dounane, Omar / Sardin, Elodie / Huvent, Isabelle / Schmitt, Alain / Hamdane, Malika / Buée, Luc / Landrieu, Isabelle / Lippens, Guy / Baulieu, Etienne Emile / Chambraud, Béatrice

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

2015 Volume 29, Issue 8, Page(s) 3171–3181

Abstract: Tauopathies, including Alzheimer's disease (AD), are neurodegenerative diseases associated with the pathologic aggregation of human brain Tau protein. Neuronal Tau is involved in microtubule (MT) formation and stabilization. We showed previously that the ...

Abstract	Tauopathies, including Alzheimer's disease (AD), are neurodegenerative diseases associated with the pathologic aggregation of human brain Tau protein. Neuronal Tau is involved in microtubule (MT) formation and stabilization. We showed previously that the immunophilin FK506-binding protein of MW ∼52 kDa (FKBP52) interferes with this function of full-length Tau and provokes aggregation of a disease-related mutant of Tau. To dissect the molecular interaction between recombinant human FKBP52 and Tau, here, we study the effect of FKBP52 on a functional Tau fragment (Tau-F4, Ser(208)-Ser(324)) containing part of the proline- rich region and MT-binding repeats. Therefore, we perform MT assembly and light-scattering assays, blue native PAGE analysis, electron microscopy, and Tau seeding experiments in SH-SY5Y human neuroblastoma cells. We show that FKBP52 (6 µM) prevents MT formation generated by Tau-F4 (5 µM) and induces Tau-F4 oligomerization and aggregation. Electron microscopy analyses show granular oligomers and filaments of Tau-F4 after short-time FKBP52 incubation. We demonstrate that the terminal parts of Tau interfere with the effects of FKBP52. Finally, we find that FKBP52-induced Tau-F4 oligomers cannot only generate in vitro, direct conformational changes in full-length Tau and that their uptake into neuronal cells can equally lead to aggregation of wild-type endogenous Tau. This suggests a potential prion-like property of these particular Tau-F4 aggregates. Collectively, our results strengthen the hypothesis of FKBP52 involvement in the Tau pathogenicity process.
MeSH term(s)	Alzheimer Disease/metabolism ; Animals ; Brain/metabolism ; Cell Line, Tumor ; Humans ; Male ; Microtubules/metabolism ; Prions/metabolism ; Protein Binding/physiology ; Rats ; Rats, Sprague-Dawley ; Tacrolimus Binding Proteins/metabolism ; Tauopathies/metabolism ; tau Proteins/metabolism
Chemical Substances	Prions ; tau Proteins ; Tacrolimus Binding Proteins (EC 5.2.1.-) ; tacrolimus binding protein 4 (EC 5.2.1.-)
Language	English
Publishing date	2015-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	639186-2
ISSN	1530-6860 ; 0892-6638
ISSN (online)	1530-6860
ISSN	0892-6638
DOI	10.1096/fj.14-268243
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Zs.A 2266: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 296: Show issues

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