Aggregation of FET proteins as a pathological change in amyotrophic lateral sclerosis (2024)

Furukawa, Y. (2017). Aggregation of FET proteins as a pathological change in amyotrophic lateral sclerosis. In Advances in Experimental Medicine and Biology (pp. 1-12). (Advances in Experimental Medicine and Biology; Vol. 925). Springer New York LLC. https://doi.org/10.1007/5584_2016_32

Furukawa, Yoshiaki ; Tokuda, Eiichi. / Aggregation of FET proteins as a pathological change in amyotrophic lateral sclerosis. Advances in Experimental Medicine and Biology. Springer New York LLC, 2017. pp. 1-12 (Advances in Experimental Medicine and Biology).

@inbook{59d131c51dd44dd6b7c1f2898b6ddfc9,

title = "Aggregation of FET proteins as a pathological change in amyotrophic lateral sclerosis",

abstract = "Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron disease that is characterized by the formation of abnormal inclusions in neurons. While the pathomechanism of ALS remains obscure, a number of proteins have been identified in the inclusion bodies, and the pathological roles of RNA-binding proteins have been increasingly emphasized. Among those, the FET proteins (FUS, EWSR1, TAF15) were recently identified as RNA-binding proteins in pathological inclusions of ALS and other neurodegenerative diseases; moreover, mutations in the genes encoding the FET proteins were found to be associated with familial forms of ALS. FET proteins are normally localized in the nucleus, but the introduction of pathogenic mutations in FET proteins leads to their abnormal redistribution to the cytoplasm, where they form aggregates. While further investigation will be required to understand the intracellular factors controlling the aggregation propensities of FET proteins, they are thought to lose their physiological functions and become toxic through their misfolding/aggregation. Here, we will briefly review recent advances of our understanding of the physiological functions and aggregation behavior of FET proteins in vivo as well as in vitro.",

keywords = "Amyotrophic lateral sclerosis, FET family proteins, FUS, Neurodegenerative diseases, Protein aggregation",

author = "Yoshiaki Furukawa and Eiichi Tokuda",

note = "Publisher Copyright: {\textcopyright} 2016, Springer International Publishing Switzerland.",

year = "2017",

doi = "10.1007/5584_2016_32",

language = "English",

series = "Advances in Experimental Medicine and Biology",

publisher = "Springer New York LLC",

pages = "1--12",

booktitle = "Advances in Experimental Medicine and Biology",

}

Furukawa, Y 2017, Aggregation of FET proteins as a pathological change in amyotrophic lateral sclerosis. in Advances in Experimental Medicine and Biology. Advances in Experimental Medicine and Biology, vol. 925, Springer New York LLC, pp. 1-12. https://doi.org/10.1007/5584_2016_32

Aggregation of FET proteins as a pathological change in amyotrophic lateral sclerosis. / Furukawa, Yoshiaki; Tokuda, Eiichi.
Advances in Experimental Medicine and Biology. Springer New York LLC, 2017. p. 1-12 (Advances in Experimental Medicine and Biology; Vol. 925).

Research output: Chapter in Book/Report/Conference proceeding › Chapter › peer-review

TY - CHAP

T1 - Aggregation of FET proteins as a pathological change in amyotrophic lateral sclerosis

AU - Furukawa, Yoshiaki

AU - Tokuda, Eiichi

N1 - Publisher Copyright:© 2016, Springer International Publishing Switzerland.

PY - 2017

Y1 - 2017

N2 - Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron disease that is characterized by the formation of abnormal inclusions in neurons. While the pathomechanism of ALS remains obscure, a number of proteins have been identified in the inclusion bodies, and the pathological roles of RNA-binding proteins have been increasingly emphasized. Among those, the FET proteins (FUS, EWSR1, TAF15) were recently identified as RNA-binding proteins in pathological inclusions of ALS and other neurodegenerative diseases; moreover, mutations in the genes encoding the FET proteins were found to be associated with familial forms of ALS. FET proteins are normally localized in the nucleus, but the introduction of pathogenic mutations in FET proteins leads to their abnormal redistribution to the cytoplasm, where they form aggregates. While further investigation will be required to understand the intracellular factors controlling the aggregation propensities of FET proteins, they are thought to lose their physiological functions and become toxic through their misfolding/aggregation. Here, we will briefly review recent advances of our understanding of the physiological functions and aggregation behavior of FET proteins in vivo as well as in vitro.

AB - Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron disease that is characterized by the formation of abnormal inclusions in neurons. While the pathomechanism of ALS remains obscure, a number of proteins have been identified in the inclusion bodies, and the pathological roles of RNA-binding proteins have been increasingly emphasized. Among those, the FET proteins (FUS, EWSR1, TAF15) were recently identified as RNA-binding proteins in pathological inclusions of ALS and other neurodegenerative diseases; moreover, mutations in the genes encoding the FET proteins were found to be associated with familial forms of ALS. FET proteins are normally localized in the nucleus, but the introduction of pathogenic mutations in FET proteins leads to their abnormal redistribution to the cytoplasm, where they form aggregates. While further investigation will be required to understand the intracellular factors controlling the aggregation propensities of FET proteins, they are thought to lose their physiological functions and become toxic through their misfolding/aggregation. Here, we will briefly review recent advances of our understanding of the physiological functions and aggregation behavior of FET proteins in vivo as well as in vitro.

KW - Amyotrophic lateral sclerosis

KW - FET family proteins

KW - FUS

KW - Neurodegenerative diseases

KW - Protein aggregation

UR - http://www.scopus.com/inward/record.url?scp=85019257415&partnerID=8YFLogxK

U2 - 10.1007/5584_2016_32

DO - 10.1007/5584_2016_32

M3 - Chapter

C2 - 27311318

AN - SCOPUS:85019257415

T3 - Advances in Experimental Medicine and Biology

SP - 1

EP - 12

BT - Advances in Experimental Medicine and Biology

PB - Springer New York LLC

ER -

Furukawa Y, Tokuda E. Aggregation of FET proteins as a pathological change in amyotrophic lateral sclerosis. In Advances in Experimental Medicine and Biology. Springer New York LLC. 2017. p. 1-12. (Advances in Experimental Medicine and Biology). doi: 10.1007/5584_2016_32