Cargando…

FUS is sequestered in nuclear aggregates in ALS patient fibroblasts

Mutations in the RNA-binding protein FUS have been shown to cause the neurodegenerative disease amyotrophic lateral sclerosis (ALS). We investigate whether mutant FUS protein in ALS patient–derived fibroblasts affects normal FUS functions in the nucleus. We investigated fibroblasts from two ALS pati...

Descripción completa

Detalles Bibliográficos
Autores principales:	Schwartz, Jacob C., Podell, Elaine R., Han, Steve S. W., Berry, James D., Eggan, Kevin C., Cech, Thomas R.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	The American Society for Cell Biology 2014
Materias:	Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4148247/ https://www.ncbi.nlm.nih.gov/pubmed/25009283 http://dx.doi.org/10.1091/mbc.E14-05-1007

Ejemplares similares

ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules
por: Vance, Caroline, et al.
Publicado: (2013)

Nucleic acid-binding specificity of human FUS protein
por: Wang, Xueyin, et al.
Publicado: (2015)

Aberrant Phase Separation of FUS Leads to Lysosome Sequestering and Acidification
por: Trnka, Franziska, et al.
Publicado: (2021)

ALS/FTD-associated protein FUS induces mitochondrial dysfunction by preferentially sequestering respiratory chain complex mRNAs
por: Tsai, Yueh-Lin, et al.
Publicado: (2020)

ALS-linked cytoplasmic FUS assemblies are compositionally different from physiological stress granules and sequester hnRNPA3, a novel modifier of FUS toxicity
por: An, Haiyan, et al.
Publicado: (2022)

FUS inclusions disrupt RNA localization by sequestering kinesin-1 and inhibiting microtubule detyrosination
por: Yasuda, Kyota, et al.
Publicado: (2017)

Molecular Determinants and Genetic Modifiers of Aggregation and Toxicity for the ALS Disease Protein FUS/TLS
por: Sun, Zhihui, et al.
Publicado: (2011)

FUS-NLS/Transportin 1 Complex Structure Provides Insights into the Nuclear Targeting Mechanism of FUS and the Implications in ALS
por: Niu, Chunyan, et al.
Publicado: (2012)

Aggregated NETs Sequester and Detoxify Extracellular Histones
por: Knopf, Jasmin, et al.
Publicado: (2019)

Does ALS‐FUS without FUS mutation represent ALS‐FET? Report of three cases
por: Borrego‐Écija, S., et al.
Publicado: (2018)

Aggregation-prone TDP-43 sequesters and drives pathological transitions of free nuclear TDP-43
por: Keating, Sean S., et al.
Publicado: (2023)

ALS-Related Mutant SOD1 Aggregates Interfere with Mitophagy by Sequestering the Autophagy Receptor Optineurin
por: Tak, Yeong Jin, et al.
Publicado: (2020)

Frameshift peptides alter the properties of truncated FUS proteins in ALS-FUS
por: An, Haiyan, et al.
Publicado: (2020)

Impaired DNA damage response signaling by FUS-NLS mutations leads to neurodegeneration and FUS aggregate formation
por: Naumann, Marcel, et al.
Publicado: (2018)

ALS/FTD-Linked Mutation in FUS Suppresses Intra-axonal Protein Synthesis and Drives Disease Without Nuclear Loss-of-Function of FUS
por: López-Erauskin, Jone, et al.
Publicado: (2018)

ALS/FTD-Linked Mutation in FUS Suppresses Intra-axonal Protein Synthesis and Drives Disease Without Nuclear Loss-of-Function of FUS
por: López-Erauskin, Jone, et al.
Publicado: (2020)

Mechanism of karyopherin-β2 binding and nuclear import of ALS variants FUS(P525L) and FUS(R495X)
por: Gonzalez, Abner, et al.
Publicado: (2021)

Nuclear RNA transcript levels modulate nucleocytoplasmic distribution of ALS/FTD-associated protein FUS
por: Tsai, Yueh-Lin, et al.
Publicado: (2022)

ALS-FUS pathology revisited: singleton FUS mutations and an unusual case with both a FUS and TARDBP mutation
por: King, Andrew, et al.
Publicado: (2015)

Mutation in TERT separates processivity from anchor-site function
por: Zaug, Arthur J, et al.
Publicado: (2008)

TLS/FUS: A protein in cancer and ALS
por: Tan, Adelene Y., et al.
Publicado: (2012)

ALS-Associated FUS Mutations Result in Compromised FUS Alternative Splicing and Autoregulation
por: Zhou, Yueqin, et al.
Publicado: (2013)

Binding of the nuclear ribonucleoprotein family member FUS to RNA prevents R-loop RNA:DNA hybrid structures
por: Thompson, Valery F., et al.
Publicado: (2023)

Identities of Sequestered Proteins in Aggregates from Cells with Induced Polyglutamine Expression
por: Suhr, Steven T., et al.
Publicado: (2001)

FUS ALS-causative mutations impair FUS autoregulation and splicing factor networks through intron retention
por: Humphrey, Jack, et al.
Publicado: (2020)

FUS mutations dominate TBK1 mutations in FUS/TBK1 double-mutant ALS/FTD pedigrees
por: Brenner, David, et al.
Publicado: (2021)

Importance of Functional Loss of FUS in FTLD/ALS
por: Ishigaki, Shinsuke, et al.
Publicado: (2018)

ALS-causative mutations in FUS/TLS confer gain- and loss-of-function by altered association with SMN and U1-snRNP
por: Sun, Shuying, et al.
Publicado: (2015)

ALS mutations in TLS/FUS disrupt target gene expression
por: Coady, Tristan H., et al.
Publicado: (2015)

Pathogenesis of FUS-associated ALS and FTD: insights from rodent models
por: Nolan, Matthew, et al.
Publicado: (2016)

Wild-type FUS corrects ALS-like disease induced by cytoplasmic mutant FUS through autoregulation
por: Sanjuan-Ruiz, Inmaculada, et al.
Publicado: (2021)

Conformational change of RNA-helicase DHX30 by ALS/FTD-linked FUS induces mitochondrial dysfunction and cytosolic aggregates
por: Hikiami, Ryota, et al.
Publicado: (2022)

Characterization of design grammar of peptides for regulating liquid droplets and aggregates of FUS
por: Kamagata, Kiyoto, et al.
Publicado: (2021)

Potential Therapeutic Role of HDAC Inhibitors in FUS-ALS
por: Tejido, Clara, et al.
Publicado: (2021)

Changes to the TDP-43 and FUS Interactomes Induced by DNA Damage
por: Kawaguchi, Tetsuya, et al.
Publicado: (2019)

Hsp70 Inhibits the Nucleation and Elongation of Tau and Sequesters Tau Aggregates with High Affinity
por: Kundel, Franziska, et al.
Publicado: (2018)

Co-factor-free aggregation of tau into seeding-competent RNA-sequestering amyloid fibrils
por: Chakraborty, Pijush, et al.
Publicado: (2021)

Recruitment into stress granules prevents irreversible aggregation of FUS protein mislocalized to the cytoplasm
por: Shelkovnikova, Tatyana A, et al.
Publicado: (2013)

FUS/TLS acts as an aggregation-dependent modifier of polyglutamine disease model mice
por: Kino, Yoshihiro, et al.
Publicado: (2016)

Phosphorylation of the FUS low‐complexity domain disrupts phase separation, aggregation, and toxicity
por: Monahan, Zachary, et al.
Publicado: (2017)

Cannot write session to /tmp/vufind_sessions/sess_ltgjmtfb3k5l4s5hsbg5sojaq5