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Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates. / Velizhanina, Maria E.; Galkin, Alexey P.

In: International Journal of Molecular Sciences, Vol. 23, No. 14, 7997, 20.07.2022.

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@article{94ce9ef2814247ab83209be76b6c861a,
title = "Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates",
abstract = "Functional amyloids are fibrillary proteins with a cross-β structure that play a structural or regulatory role in pro- and eukaryotes. Previously, we have demonstrated that the RNA-binding FXR1 protein functions in an amyloid form in the rat brain. This RNA-binding protein plays an important role in the regulation of long-term memory, emotions, and cancer. Here, we evaluate the amyloid properties of FXR1 in organisms representing various classes of vertebrates. We show the colocalization of FXR1 with amyloid-specific dyes in the neurons of amphibians, reptiles, and birds. Moreover, FXR1, as with other amyloids, forms detergent-resistant insoluble aggregates in all studied animals. The FXR1 protein isolated by immunoprecipitation from the brains of different vertebrate species forms fibrils, which show yellow-green birefringence after staining with Congo red. Our data indicate that in the evolution of vertebrates, FXR1 acquired amyloid properties at least 365 million years ago. Based on the obtained data, we discuss the possible role of FXR1 amyloid fibrils in the regulation of vital processes in the brain of vertebrates.",
keywords = "amphibians, birds, brain, evolution, fish, functional amyloid, FXR1 protein, mammals, reptiles, vertebrates",
author = "Velizhanina, {Maria E.} and Galkin, {Alexey P.}",
year = "2022",
month = jul,
day = "20",
doi = "10.3390/ijms23147997",
language = "English",
volume = "23",
journal = "International Journal of Molecular Sciences",
issn = "1422-0067",
publisher = "MDPI AG",
number = "14",

}

RIS

TY - JOUR

T1 - Amyloid Properties of the FXR1 Protein Are Conserved in Evolution of Vertebrates

AU - Velizhanina, Maria E.

AU - Galkin, Alexey P.

PY - 2022/7/20

Y1 - 2022/7/20

N2 - Functional amyloids are fibrillary proteins with a cross-β structure that play a structural or regulatory role in pro- and eukaryotes. Previously, we have demonstrated that the RNA-binding FXR1 protein functions in an amyloid form in the rat brain. This RNA-binding protein plays an important role in the regulation of long-term memory, emotions, and cancer. Here, we evaluate the amyloid properties of FXR1 in organisms representing various classes of vertebrates. We show the colocalization of FXR1 with amyloid-specific dyes in the neurons of amphibians, reptiles, and birds. Moreover, FXR1, as with other amyloids, forms detergent-resistant insoluble aggregates in all studied animals. The FXR1 protein isolated by immunoprecipitation from the brains of different vertebrate species forms fibrils, which show yellow-green birefringence after staining with Congo red. Our data indicate that in the evolution of vertebrates, FXR1 acquired amyloid properties at least 365 million years ago. Based on the obtained data, we discuss the possible role of FXR1 amyloid fibrils in the regulation of vital processes in the brain of vertebrates.

AB - Functional amyloids are fibrillary proteins with a cross-β structure that play a structural or regulatory role in pro- and eukaryotes. Previously, we have demonstrated that the RNA-binding FXR1 protein functions in an amyloid form in the rat brain. This RNA-binding protein plays an important role in the regulation of long-term memory, emotions, and cancer. Here, we evaluate the amyloid properties of FXR1 in organisms representing various classes of vertebrates. We show the colocalization of FXR1 with amyloid-specific dyes in the neurons of amphibians, reptiles, and birds. Moreover, FXR1, as with other amyloids, forms detergent-resistant insoluble aggregates in all studied animals. The FXR1 protein isolated by immunoprecipitation from the brains of different vertebrate species forms fibrils, which show yellow-green birefringence after staining with Congo red. Our data indicate that in the evolution of vertebrates, FXR1 acquired amyloid properties at least 365 million years ago. Based on the obtained data, we discuss the possible role of FXR1 amyloid fibrils in the regulation of vital processes in the brain of vertebrates.

KW - amphibians

KW - birds

KW - brain

KW - evolution

KW - fish

KW - functional amyloid

KW - FXR1 protein

KW - mammals

KW - reptiles

KW - vertebrates

UR - http://www.scopus.com/inward/record.url?scp=85135126792&partnerID=8YFLogxK

U2 - 10.3390/ijms23147997

DO - 10.3390/ijms23147997

M3 - Article

C2 - 35887344

AN - SCOPUS:85135126792

VL - 23

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 14

M1 - 7997

ER -

ID: 102041083