Cargando…

Glial TDP-43 regulates axon wrapping, GluRIIA clustering and fly motility by autonomous and non-autonomous mechanisms

Alterations in the glial function of TDP-43 are becoming increasingly associated with the neurological symptoms observed in Amyotrophic Lateral Sclerosis (ALS), however, the physiological role of this protein in the glia or the mechanisms that may lead to neurodegeneration are unknown. To address th...

Descripción completa

Detalles Bibliográficos
Autores principales:	Romano, Giulia, Appocher, Chiara, Scorzeto, Michele, Klima, Raffaella, Baralle, Francisco E., Megighian, Aram, Feiguin, Fabian
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Oxford University Press 2015
Materias:	Articles
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4599672/ https://www.ncbi.nlm.nih.gov/pubmed/26276811 http://dx.doi.org/10.1093/hmg/ddv330

Ejemplares similares

Precise mapping of one classic and three novel GluRIIA mutants in Drosophila melanogaster
por: Mallik, Bhagaban, et al.
Publicado: (2023)

Anterograde Activin Signaling Regulates Postsynaptic Membrane Potential and GluRIIA/B Abundance at the Drosophila Neuromuscular Junction
por: Kim, Myung-Jun, et al.
Publicado: (2014)

TDP-43 Regulates Drosophila Neuromuscular Junctions Growth by Modulating Futsch/MAP1B Levels and Synaptic Microtubules Organization
por: Godena, Vinay K., et al.
Publicado: (2011)

Staufen targets coracle mRNA to Drosophila neuromuscular junctions and regulates GluRIIA synaptic accumulation and bouton number
por: Gardiol, Alejandra, et al.
Publicado: (2014)

TDP-43 promotes the formation of neuromuscular synapses through the regulation of Disc-large expression in Drosophila skeletal muscles
por: Strah, Nina, et al.
Publicado: (2020)

Major hnRNP proteins act as general TDP-43 functional modifiers both in Drosophila and human neuronal cells
por: Appocher, Chiara, et al.
Publicado: (2017)

Drosophila Answers to TDP-43 Proteinopathies
por: Romano, Maurizio, et al.
Publicado: (2012)

TDP-43 prevents retrotransposon activation in the Drosophila motor system through regulation of Dicer-2 activity
por: Romano, Giulia, et al.
Publicado: (2020)

TDP-43 regulates GAD1 mRNA splicing and GABA signaling in Drosophila CNS
por: Romano, Giulia, et al.
Publicado: (2021)

A novel Drosophila model of TDP-43 proteinopathies: N-terminal sequences combined with the Q/N domain induce protein functional loss and locomotion defects
por: Langellotti, Simona, et al.
Publicado: (2016)

TDP-43 aggregation mirrors TDP-43 knockdown, affecting the expression levels of a common set of proteins
por: Prpar Mihevc, S., et al.
Publicado: (2016)

Characterizing TDP-43 interaction with its RNA targets
por: Bhardwaj, Amit, et al.
Publicado: (2013)

Downregulation of glutamic acid decarboxylase in Drosophila TDP-43-null brains provokes paralysis by affecting the organization of the neuromuscular synapses
por: Romano, Giulia, et al.
Publicado: (2018)

Transactivation Response DNA-Binding Protein of 43 (TDP-43) and Glial Cell Roles in Neurological Disorders
por: Hussain, Hussain, et al.
Publicado: (2022)

An Amyloid-Like Pathological Conformation of TDP-43 Is Stabilized by Hypercooperative Hydrogen Bonds
por: Mompeán, Miguel, et al.
Publicado: (2016)

Predominance of spliceosomal complex formation over polyadenylation site selection in TDP-43 autoregulation
por: Bembich, Sara, et al.
Publicado: (2014)

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

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

Physiological tissue-specific and age-related reduction of mouse TDP-43 levels is regulated by epigenetic modifications
por: Pacetti, Miriam, et al.
Publicado: (2022)

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

Functional mapping of the interaction between TDP-43 and hnRNP A2 in vivo
por: D’Ambrogio, Andrea, et al.
Publicado: (2009)

Rodent Models of TDP-43 Proteinopathy: Investigating the Mechanisms of TDP-43-Mediated Neurodegeneration
por: Gendron, Tania F., et al.
Publicado: (2011)

Chaperone Mediated Autophagy Degrades TDP-43 Protein and Is Affected by TDP-43 Aggregation
por: Ormeño, Fernando, et al.
Publicado: (2020)

The synaptotagmin juxtamembrane domain is involved in neuroexocytosis
por: Caccin, Paola, et al.
Publicado: (2015)

Formation and spreading of TDP-43 aggregates in cultured neuronal and glial cells demonstrated by time-lapse imaging
por: Ishii, Tomohiro, et al.
Publicado: (2017)

Su(var)3-9 mediates age-dependent increase in H3K9 methylation on TDP-43 promoter triggering neurodegeneration
por: Marzullo, Marta, et al.
Publicado: (2023)

TDP-43 crosses the divide
por: Leslie, Mitch
Publicado: (2015)

Loss of ISWI Function in Drosophila Nuclear Bodies Drives Cytoplasmic Redistribution of Drosophila TDP-43
por: Lo Piccolo, Luca, et al.
Publicado: (2018)

TDP-43: From Alzheimer’s Disease to Limbic-Predominant Age-Related TDP-43 Encephalopathy
por: Huang, Wendi, et al.
Publicado: (2020)

TDP-43 mislocalization drives neurofilament changes in a novel model of TDP-43 proteinopathy
por: Atkinson, Rachel, et al.
Publicado: (2021)

The cooperative binding of TDP-43 to GU-rich RNA repeats antagonizes TDP-43 aggregation
por: Rengifo-Gonzalez, Juan Carlos, et al.
Publicado: (2021)

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

NOS1AP is a novel molecular target and critical factor in TDP-43 pathology
por: Cappelli, Sara, et al.
Publicado: (2022)

Evidence of cerebellar TDP-43 loss of function in FTLD-TDP
por: Pickles, Sarah, et al.
Publicado: (2022)

TDP-43 affects splicing profiles and isoform production of genes involved in the apoptotic and mitotic cellular pathways
por: De Conti, Laura, et al.
Publicado: (2015)

Depletion of TDP 43 overrides the need for exonic and intronic splicing enhancers in the human apoA-II gene
por: Mercado, Pablo Arrisi, et al.
Publicado: (2005)

Antibody against TDP-43 phosphorylated at serine 375 suggests conformational differences of TDP-43 aggregates among FTLD–TDP subtypes
por: Neumann, Manuela, et al.
Publicado: (2020)

The Pathological Phenotypes of Human TDP-43 Transgenic Mouse Models Are Independent of Downregulation of Mouse Tdp-43
por: Xu, Ya-Fei, et al.
Publicado: (2013)

TDP-43 and Phosphorylated TDP-43 Levels in Paired Plasma and CSF Samples in Amyotrophic Lateral Sclerosis
por: Ren, Yuting, et al.
Publicado: (2021)

TREM2 interacts with TDP-43 and mediates microglial neuroprotection against TDP-43-related neurodegeneration
por: Xie, Manling, et al.
Publicado: (2021)

Cannot write session to /tmp/vufind_sessions/sess_cnrlo2srusl1sot35na2c0bu7d