Cargando…

Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1

TDP-43 and FUS are nuclear proteins with multiple functions in mRNA processing. They play key roles in ALS (amyotrophic lateral sclerosis) and FTD (frontotemporal dementia), where they are partially lost from the nucleus and aggregate in the cytoplasm of neurons and glial cells. Defects in nucleocyt...

Descripción completa

Detalles Bibliográficos
Autores principales:	Ederle, Helena, Funk, Christina, Abou-Ajram, Claudia, Hutten, Saskia, Funk, Eva B. E., Kehlenbach, Ralph H., Bailer, Susanne M., Dormann, Dorothee
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group UK 2018
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5935713/ https://www.ncbi.nlm.nih.gov/pubmed/29728564 http://dx.doi.org/10.1038/s41598-018-25007-5

Ejemplares similares

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation
por: Gruijs da Silva, Lara A, et al.
Publicado: (2022)

The RNA-binding protein FUS is chaperoned and imported into the nucleus by a network of import receptors
por: Baade, Imke, et al.
Publicado: (2021)

Structural Basis of Targeting the Exportin CRM1 in Cancer
por: Dickmanns, Achim, et al.
Publicado: (2015)

Neuropathological potential of FUS and TDP-43 in flies
Publicado: (2011)

Allosteric control of the exportin CRM1 unraveled by crystal structure analysis
por: Monecke, Thomas, et al.
Publicado: (2014)

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

Cytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD
por: Khosravi, Bahram, et al.
Publicado: (2017)

Structural determinants of nuclear export signal orientation in binding to exportin CRM1
por: Fung, Ho Yee Joyce, et al.
Publicado: (2015)

Tubulin is actively exported from the nucleus through the Exportin1/CRM1 pathway
por: Schwarzerová, K., et al.
Publicado: (2019)

Sustained Expression of TDP-43 and FUS in Motor Neurons in Rodent's Lifetime
por: Huang, Cao, et al.
Publicado: (2010)

Ubiquitin Homeostasis Is Disrupted in TDP-43 and FUS Cell Models of ALS
por: Farrawell, Natalie E., et al.
Publicado: (2020)

Frequency of ubiquitin and FUS-positive, TDP-43-negative frontotemporal lobar degeneration
por: Seelaar, Harro, et al.
Publicado: (2009)

Synaptic Paths to Neurodegeneration: The Emerging Role of TDP-43 and FUS in Synaptic Functions
por: Ling, Shuo-Chien
Publicado: (2018)

Rescue of Mitochondrial Function in Hutchinson-Gilford Progeria Syndrome by the Pharmacological Modulation of Exportin CRM1
por: Monterrubio-Ledezma, Feliciano, et al.
Publicado: (2023)

Aberrant Localization of FUS and TDP43 Is Associated with Misfolding of SOD1 in Amyotrophic Lateral Sclerosis
por: Pokrishevsky, Edward, et al.
Publicado: (2012)

Oxr1 improves pathogenic cellular features of ALS-associated FUS and TDP-43 mutations
por: Finelli, Mattéa J., et al.
Publicado: (2015)

Distinct partitioning of ALS associated TDP-43, FUS and SOD1 mutants into cellular inclusions
por: Farrawell, Natalie E., et al.
Publicado: (2015)

FUS pathology defines the majority of tau- and TDP-43-negative frontotemporal lobar degeneration
por: Urwin, Hazel, et al.
Publicado: (2010)

Mutant TDP-43 and FUS Cause Age-Dependent Paralysis and Neurodegeneration in C. elegans
por: Vaccaro, Alexandra, et al.
Publicado: (2012)

Liquid-Liquid Phase Separation of TDP-43 and FUS in Physiology and Pathology of Neurodegenerative Diseases
por: Carey, Jenny L., et al.
Publicado: (2022)

Exportin Crm1 is repurposed as a docking protein to generate microtubule organizing centers at the nuclear pore
por: Bao, Xun X, et al.
Publicado: (2018)

Exportin Crm1 is important for Swi6 nuclear shuttling and MBF transcription activation in Saccharomyces cerevisiae
por: Belanger, Kenneth D., et al.
Publicado: (2022)

Diffuse argyrophilic grain disease with TDP-43 proteinopathy and neuronal intermediate filament inclusion disease: FTLD with mixed tau, TDP-43 and FUS pathologies
por: Koga, Shunsuke, et al.
Publicado: (2023)

Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP
por: Aulas, Anaïs, et al.
Publicado: (2012)

Mining Disaggregase Sequence Space to Safely Counter TDP-43, FUS, and α-Synuclein Proteotoxicity
por: Tariq, Amber, et al.
Publicado: (2019)

Enhanced Activity of Exportin-1/CRM1 in Neurons Contributes to Autophagy Dysfunction and Senescent Features in Old Mouse Brain
por: Gorostieta-Salas, Elisa, et al.
Publicado: (2021)

Publisher Correction to: Diffuse argyrophilic grain disease with TDP-43 proteinopathy and neuronal intermediate filament inclusion disease: FTLD with mixed tau, TDP-43 and FUS pathologies
por: Koga, Shunsuke, et al.
Publicado: (2023)

Generation and analysis of innovative genomically humanized knockin SOD1, TARDBP (TDP-43), and FUS mouse models
por: Devoy, Anny, et al.
Publicado: (2021)

Generation and analysis of innovative genomically humanized knockin SOD1, TARDBP (TDP-43), and FUS mouse models
por: Devoy, Anny, et al.
Publicado: (2022)

DCTN1 Binds to TDP-43 and Regulates TDP-43 Aggregation
por: Deshimaru, Manami, et al.
Publicado: (2021)

Rrp12 and the Exportin Crm1 Participate in Late Assembly Events in the Nucleolus during 40S Ribosomal Subunit Biogenesis
por: Moriggi, Giulia, et al.
Publicado: (2014)

Methylene Blue Protects against TDP-43 and FUS Neuronal Toxicity in C. elegans and D. rerio
por: Vaccaro, Alexandra, et al.
Publicado: (2012)

Erratum to: Endogenous TDP-43, but not FUS, contributes to stress granule assembly via G3BP
por: Aulas, Anaïs, et al.
Publicado: (2015)

Alterations in stress granule dynamics driven by TDP-43 and FUS: a link to pathological inclusions in ALS?
por: Aulas, Anaïs, et al.
Publicado: (2015)

Essential Roles and Risks of G-Quadruplex Regulation: Recognition Targets of ALS-Linked TDP-43 and FUS
por: Ishiguro, Akira, et al.
Publicado: (2022)

The dependence of Ig class-switching on the nuclear export sequence of AID likely reflects interaction with factors additional to Crm1 exportin
por: Ellyard, Julia I, et al.
Publicado: (2011)

Distinct and shared functions of ALS-associated proteins TDP-43, FUS and TAF15 revealed by multisystem analyses
por: Kapeli, Katannya, et al.
Publicado: (2016)

Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivo
por: Riemenschneider, Henrick, et al.
Publicado: (2023)

TDP-43 and Limbic-Predominant Age-Related TDP-43 Encephalopathy
por: Zhang, Lumi, et al.
Publicado: (2020)

A Role for RanBP1 in the Release of CRM1 from the Nuclear Pore Complex in a Terminal Step of Nuclear Export
por: Kehlenbach, Ralph H., et al.
Publicado: (1999)

Cannot write session to /tmp/vufind_sessions/sess_mig0bnouqh60u4qc13jnehvo6a