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Cyclase-associated protein 2 dimerization regulates cofilin in synaptic plasticity and Alzheimer's disease

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Cyclase-associated protein 2 dimerization regulates cofilin in synaptic plasticity and Alzheimer's disease. / Pelucchi, Silvia; Vandermeulen, Lina; Pizzamiglio, Lara; Aksan, Bahar; Yan, Jing; Konietzny, Anja; Bonomi, Elisa; Borroni, Barbara; Padovani, Alessandro; Rust, Marco B; Di Marino, Daniele; Mikhaylova, Marina; Mauceri, Daniela; Antonucci, Flavia; Edefonti, Valeria; Gardoni, Fabrizio; Di Luca, Monica; Marcello, Elena.

In: BRAIN COMMUN, Vol. 2, No. 2, 26.06.2020, p. fcaa086.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Pelucchi, S, Vandermeulen, L, Pizzamiglio, L, Aksan, B, Yan, J, Konietzny, A, Bonomi, E, Borroni, B, Padovani, A, Rust, MB, Di Marino, D, Mikhaylova, M, Mauceri, D, Antonucci, F, Edefonti, V, Gardoni, F, Di Luca, M & Marcello, E 2020, 'Cyclase-associated protein 2 dimerization regulates cofilin in synaptic plasticity and Alzheimer's disease', BRAIN COMMUN, vol. 2, no. 2, pp. fcaa086. https://doi.org/10.1093/braincomms/fcaa086

APA

Pelucchi, S., Vandermeulen, L., Pizzamiglio, L., Aksan, B., Yan, J., Konietzny, A., Bonomi, E., Borroni, B., Padovani, A., Rust, M. B., Di Marino, D., Mikhaylova, M., Mauceri, D., Antonucci, F., Edefonti, V., Gardoni, F., Di Luca, M., & Marcello, E. (2020). Cyclase-associated protein 2 dimerization regulates cofilin in synaptic plasticity and Alzheimer's disease. BRAIN COMMUN, 2(2), fcaa086. https://doi.org/10.1093/braincomms/fcaa086

Vancouver

Pelucchi S, Vandermeulen L, Pizzamiglio L, Aksan B, Yan J, Konietzny A et al. Cyclase-associated protein 2 dimerization regulates cofilin in synaptic plasticity and Alzheimer's disease. BRAIN COMMUN. 2020 Jun 26;2(2):fcaa086. https://doi.org/10.1093/braincomms/fcaa086

Bibtex

@article{6b734efd63374ecd843d91c8c55bb614,
title = "Cyclase-associated protein 2 dimerization regulates cofilin in synaptic plasticity and Alzheimer's disease",
abstract = "Regulation of actin cytoskeleton dynamics in dendritic spines is crucial for learning and memory formation. Hence, defects in the actin cytoskeleton pathways are a biological trait of several brain diseases, including Alzheimer's disease. Here, we describe a novel synaptic mechanism governed by the cyclase-associated protein 2, which is required for structural plasticity phenomena and completely disrupted in Alzheimer's disease. We report that the formation of cyclase-associated protein 2 dimers through its Cys32 is important for cyclase-associated protein 2 binding to cofilin and for actin turnover. The Cys32-dependent cyclase-associated protein 2 homodimerization and association to cofilin are triggered by long-term potentiation and are required for long-term potentiation-induced cofilin translocation into spines, spine remodelling and the potentiation of synaptic transmission. This mechanism is specifically affected in the hippocampus, but not in the superior frontal gyrus, of both Alzheimer's disease patients and APP/PS1 mice, where cyclase-associated protein 2 is down-regulated and cyclase-associated protein 2 dimer synaptic levels are reduced. Notably, cyclase-associated protein 2 levels in the cerebrospinal fluid are significantly increased in Alzheimer's disease patients but not in subjects affected by frontotemporal dementia. In Alzheimer's disease hippocampi, cofilin association to cyclase-associated protein 2 dimer/monomer is altered and cofilin is aberrantly localized in spines. Taken together, these results provide novel insights into structural plasticity mechanisms that are defective in Alzheimer's disease.",
author = "Silvia Pelucchi and Lina Vandermeulen and Lara Pizzamiglio and Bahar Aksan and Jing Yan and Anja Konietzny and Elisa Bonomi and Barbara Borroni and Alessandro Padovani and Rust, {Marco B} and {Di Marino}, Daniele and Marina Mikhaylova and Daniela Mauceri and Flavia Antonucci and Valeria Edefonti and Fabrizio Gardoni and {Di Luca}, Monica and Elena Marcello",
note = "{\textcopyright} The Author(s) (2020). Published by Oxford University Press on behalf of the Guarantors of Brain.",
year = "2020",
month = jun,
day = "26",
doi = "10.1093/braincomms/fcaa086",
language = "English",
volume = "2",
pages = "fcaa086",
journal = "BRAIN COMMUN",
issn = "2632-1297",
publisher = "OXFORD UNIV PRESS",
number = "2",

}

RIS

TY - JOUR

T1 - Cyclase-associated protein 2 dimerization regulates cofilin in synaptic plasticity and Alzheimer's disease

AU - Pelucchi, Silvia

AU - Vandermeulen, Lina

AU - Pizzamiglio, Lara

AU - Aksan, Bahar

AU - Yan, Jing

AU - Konietzny, Anja

AU - Bonomi, Elisa

AU - Borroni, Barbara

AU - Padovani, Alessandro

AU - Rust, Marco B

AU - Di Marino, Daniele

AU - Mikhaylova, Marina

AU - Mauceri, Daniela

AU - Antonucci, Flavia

AU - Edefonti, Valeria

AU - Gardoni, Fabrizio

AU - Di Luca, Monica

AU - Marcello, Elena

N1 - © The Author(s) (2020). Published by Oxford University Press on behalf of the Guarantors of Brain.

PY - 2020/6/26

Y1 - 2020/6/26

N2 - Regulation of actin cytoskeleton dynamics in dendritic spines is crucial for learning and memory formation. Hence, defects in the actin cytoskeleton pathways are a biological trait of several brain diseases, including Alzheimer's disease. Here, we describe a novel synaptic mechanism governed by the cyclase-associated protein 2, which is required for structural plasticity phenomena and completely disrupted in Alzheimer's disease. We report that the formation of cyclase-associated protein 2 dimers through its Cys32 is important for cyclase-associated protein 2 binding to cofilin and for actin turnover. The Cys32-dependent cyclase-associated protein 2 homodimerization and association to cofilin are triggered by long-term potentiation and are required for long-term potentiation-induced cofilin translocation into spines, spine remodelling and the potentiation of synaptic transmission. This mechanism is specifically affected in the hippocampus, but not in the superior frontal gyrus, of both Alzheimer's disease patients and APP/PS1 mice, where cyclase-associated protein 2 is down-regulated and cyclase-associated protein 2 dimer synaptic levels are reduced. Notably, cyclase-associated protein 2 levels in the cerebrospinal fluid are significantly increased in Alzheimer's disease patients but not in subjects affected by frontotemporal dementia. In Alzheimer's disease hippocampi, cofilin association to cyclase-associated protein 2 dimer/monomer is altered and cofilin is aberrantly localized in spines. Taken together, these results provide novel insights into structural plasticity mechanisms that are defective in Alzheimer's disease.

AB - Regulation of actin cytoskeleton dynamics in dendritic spines is crucial for learning and memory formation. Hence, defects in the actin cytoskeleton pathways are a biological trait of several brain diseases, including Alzheimer's disease. Here, we describe a novel synaptic mechanism governed by the cyclase-associated protein 2, which is required for structural plasticity phenomena and completely disrupted in Alzheimer's disease. We report that the formation of cyclase-associated protein 2 dimers through its Cys32 is important for cyclase-associated protein 2 binding to cofilin and for actin turnover. The Cys32-dependent cyclase-associated protein 2 homodimerization and association to cofilin are triggered by long-term potentiation and are required for long-term potentiation-induced cofilin translocation into spines, spine remodelling and the potentiation of synaptic transmission. This mechanism is specifically affected in the hippocampus, but not in the superior frontal gyrus, of both Alzheimer's disease patients and APP/PS1 mice, where cyclase-associated protein 2 is down-regulated and cyclase-associated protein 2 dimer synaptic levels are reduced. Notably, cyclase-associated protein 2 levels in the cerebrospinal fluid are significantly increased in Alzheimer's disease patients but not in subjects affected by frontotemporal dementia. In Alzheimer's disease hippocampi, cofilin association to cyclase-associated protein 2 dimer/monomer is altered and cofilin is aberrantly localized in spines. Taken together, these results provide novel insights into structural plasticity mechanisms that are defective in Alzheimer's disease.

U2 - 10.1093/braincomms/fcaa086

DO - 10.1093/braincomms/fcaa086

M3 - SCORING: Journal article

C2 - 33094279

VL - 2

SP - fcaa086

JO - BRAIN COMMUN

JF - BRAIN COMMUN

SN - 2632-1297

IS - 2

ER -