The RNA-binding protein FUS/TLS is a common aggregate-interacting protein in polyglutamine diseases.
Neuronal intranuclear inclusions (NIIs) are the pathological hallmark of polyglutamine (polyQ) diseases. We previously found that the RNA-binding protein FUS/TLS is the major component of nuclear polyQ aggregates of a cellular model of Huntington disease. In this study, we revealed that FUS/TLS binds to NIIs in the human brains from patients with spinocerebellar ataxia type 1, 2, 3, and dentatorubral-pallidoluysian atrophy. Recent reports have revealed that mutations in FUS/TLS gene are responsible for familial amyotrophic lateral sclerosis 6 (ALS6). Our results indicated that changing FUS/TLS to an insoluble form may be a common process in polyQ diseases and ALS6.
Doi
Hiroshi
H
Department of Clinical Neurology and Stroke Medicine, Graduate School of Medicine, Yokohama City University, 3-9 Fukuura, Kanazawa-ku, Yokohama 236-0004, Japan. doi@rkd.d-bs.com
Koyano
Shigeru
S
Suzuki
Yume
Y
Nukina
Nobuyuki
N
Kuroiwa
Yoshiyuki
Y
D001921:Brain / Q000378:metabolism / Q000473:pathology*; D002467:Cell Nucleus / Q000378:metabolism* / Q000473:pathology; D006801:Humans; D006816:Huntington Disease / Q000235:genetics / Q000378:metabolism / Q000473:pathology*; D009474:Neurons / Q000473:pathology; D010455:Peptides / Q000235:genetics* / Q000378:metabolism; D011180:Postmortem Changes; D034702:RNA-Binding Protein FUS / Q000235:genetics / Q000378:metabolism*
D010455:Peptides; D034702:RNA-Binding Protein FUS; C097188:polyglutamine