Yves Goldberg

ORCID: 0000-0001-7446-8595
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About
Contact & Profiles
Research Areas
  • Neuroscience and Neuropharmacology Research
  • RNA regulation and disease
  • Protein Kinase Regulation and GTPase Signaling
  • Alzheimer's disease research and treatments
  • Microtubule and mitosis dynamics
  • Cellular transport and secretion
  • RNA Research and Splicing
  • Monoclonal and Polyclonal Antibodies Research
  • Receptor Mechanisms and Signaling
  • Cancer Mechanisms and Therapy
  • Retinal Development and Disorders
  • interferon and immune responses
  • Thyroid Disorders and Treatments
  • Protein Tyrosine Phosphatases
  • Polyamine Metabolism and Applications
  • Extracellular vesicles in disease
  • Lipid Membrane Structure and Behavior
  • Cholinesterase and Neurodegenerative Diseases
  • Cancer, Hypoxia, and Metabolism
  • Histone Deacetylase Inhibitors Research
  • Growth Hormone and Insulin-like Growth Factors
  • Endoplasmic Reticulum Stress and Disease
  • Advanced Fluorescence Microscopy Techniques
  • MicroRNA in disease regulation
  • Cell death mechanisms and regulation

Inserm
2006-2025

Grenoble Institute of Neurosciences
2008-2025

Université Grenoble Alpes
2015-2025

CEA Grenoble
1999-2022

Centre National de la Recherche Scientifique
1989-2022

Commissariat à l'Énergie Atomique et aux Énergies Alternatives
1997-2022

Institut de Recherches en Technologies et Sciences pour le Vivant
2010-2018

CEA Cadarache
2018

University of Bristol
2012

Université Joseph Fourier
2005-2011

Timely deactivation of kinase cascades is crucial to the normal control cell signaling and partly accomplished by protein phosphatase 2A (PP2A). The catalytic (α) subunit serine-threonine casein 2 (CK2) bound PP2A in vitro mitogen-starved cells; binding required integrity a sequence motif common CK2α SV40 small t antigen. Overexpression resulted mitogen-activated (MEK) suppression growth. Moreover, inhibited transforming activity oncogenic Ras, but not that constitutively activated MEK....

10.1126/science.276.5314.952 article EN Science 1997-05-09

The endosomal sorting complexes required for transport (ESCRT-0-III) allow membrane budding and fission away from the cytosol. This machinery is used during multivesicular endosome biogenesis, cytokinesis, of some enveloped viruses. Membrane catalyzed by ESCRT-III made polymers charged body proteins (CHMPs) AAA-type ATPase VPS4. How which subunits sustain cytoplasmic surface remain uncertain. In vitro, CHMP2 CHMP3 recombinant polymerize into tubular helical structures, were hypothesized to...

10.1074/jbc.m111.283671 article EN cc-by Journal of Biological Chemistry 2011-09-17

Abstract Microtubules play fundamental roles in the maintenance of neuronal processes and synaptic function plasticity. While dynamic microtubules are mainly composed tyrosinated tubulin, long-lived contain detyrosinated suggesting that tubulin tyrosination/detyrosination cycle is a key player microtubule dynamics homeostasis, conditions go awry neurodegenerative diseases. In cycle, C-terminal tyrosine α-tubulin removed by carboxypeptidases re-added ligase (TTL). Here we show TTL...

10.1093/brain/awab436 article EN cc-by Brain 2021-12-13

The charged multivesicular body proteins (Chmp1–7) are an evolutionarily conserved family of cytosolic that transiently assembles into helical polymers change the curvature cellular membrane domains. Mutations in human CHMP2B cause frontotemporal dementia, suggesting this protein may normally control some neuron-specific process. Here, we examined function, localization, and interactions neuronal Chmp2b. was highly expressed mouse brain could be readily detected dendrites spines. Depletion...

10.1523/jneurosci.0586-14.2015 article EN cc-by-nc-sa Journal of Neuroscience 2015-02-18

The highly conserved ESCRT-III complex is responsible for deformation and cleavage of membranes during endosomal trafficking other cellular activities. In humans, dominant mutations in the subunit CHMP2B cause frontotemporal dementia (FTD). decade-long process leading to this cortical degeneration not well understood. One possibility that, akin neurodegenerative diseases, pathogenic protein affects integrity dendritic spines synapses before any neuronal death. Using confocal microscopy 3D...

10.1242/jcs.068817 article EN Journal of Cell Science 2010-08-11

Microtubules (MTs) support a variety of neuronal functions, such as maintenance cell structure, transport, and synaptic plasticity. Neuronal MTs are highly heterogeneous due to several tubulin isotypes the presence multiple post-translational modifications, detyrosination acetylation. The tyrosination/detyrosination cycle is key player in MT dynamics, tyrosinated associated with more dynamic MTs, while detyrosinated linked longer lived, stable MTs. Dysfunction re-tyrosination was recently...

10.3389/fcell.2022.926914 article EN cc-by Frontiers in Cell and Developmental Biology 2022-08-26

Abstract Emerging evidence indicates that microtubule-associated proteins (MAPs) are implicated in synaptic function; particular, mice deficient for MAP6 exhibit striking deficits plasticity and cognition. How connects to mechanisms is unclear. Here, we address the possible role of this protein dendritic spines. We find MAP6-deficient cortical hippocampal neurons, maintenance mature spines impaired, can be restored by expressing a stretch sequence called Mc modules. modules directly bind...

10.1038/s41467-018-05869-z article EN cc-by Nature Communications 2018-09-11

Abstract In cultured hippocampal neurons and in adult brain, the splicing regulatory protein Sam68 is partially relocated to somatodendritic domain associates with dendritic polysomes. Transfer dendrites activity‐dependent. We have investigated repertoire of neuronal mRNAs which binds vivo. By using coimmunoprecipitation microarray screening techniques, was found associate a number plasticity‐related mRNA species, including Eef1a1, an activity‐responsive coding for translation elongation...

10.1002/jnr.21824 article EN Journal of Neuroscience Research 2008-08-18

The traffic and expression of mRNAs in neurons are modulated by changes neuronal activity. regulation RNA-binding proteins is therefore currently receiving attention. Sam68 a ubiquitous nuclear protein implicated post-transcriptional processes such as signal-dependent splice site selection. We show that undergoes activity-responsive translocation to the soma dendrites hippocampal primary culture. In unstimulated transiently expressing GFP-Sam68 fusion protein, 90% cells accumulated...

10.1242/jcs.00927 article EN Journal of Cell Science 2004-03-01

Abstract The RNA‐binding protein Sam68 has been implicated in the signal‐dependent processing of pre‐mRNA and utilization intron‐containing retroviral mRNAs. is predominantly nuclear but exhibits remarkable binding affinity for signalling proteins located at membrane. We have investigated subcellular distribution adult rat cortex hippocampus. Subcellular fractionation showed that was most abundant nuclei also present a significant level cytosol membrane fractions, including light synaptic...

10.1002/jnr.20003 article EN Journal of Neuroscience Research 2004-01-26

The transcriptional activities of c-Ets-1 and v-Ets their functional interaction with the AP-1 factor c-Jun were investigated. Several recombinant Ets proteins produced purified either from bacteria or insect cells. Plasmid DNAs that contained polyoma virus enhancer Ets/AP-1 element used as templates for in vitro transcription assays presence HeLa nuclear extract various combinations Jun proteins. Under these conditions full-length on its own does not markedly influence but abolishes strong...

10.1016/s0021-9258(19)89426-7 article EN cc-by Journal of Biological Chemistry 1994-06-01

The in vitro translated products of several c-erbA cDNAs have recently been shown to bind thyroid hormones with high affinity and termed hormone receptors. We used a panel five erbA-related antibodies probe the relationship between receptors, as conventionally measured by 125I-T3 labeling nuclear extracts. All immunoprecipitated chick products, but only one them recognized liver brain T3 receptor, judged acceleration sedimentation through sucrose gradients. None reacted rat or human although...

10.1210/mend-2-10-986 article EN Molecular Endocrinology 1988-10-01
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