Jean Massoulié

Summary

Country: France

Publications

  1. doi request reprint Old and new questions about cholinesterases
    Jean Massoulié
    Laboratoire de Neurobiologie, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, Paris, France
    Chem Biol Interact 175:30-44. 2008
  2. doi request reprint Cholinesterases and the basal lamina at vertebrate neuromuscular junctions
    Jean Massoulié
    Laboratoire de Neurobiologie, UMR8544 CNRS, Ecole Normale Superieure, 46 rue d Ulm, 75005 Paris, France
    Curr Opin Pharmacol 9:316-25. 2009
  3. ncbi request reprint The origin of the molecular diversity and functional anchoring of cholinesterases
    Jean Massoulié
    CNRS UMR 8544, Laboratoire de Neurobiologie, Ecole Normale Superieure, Paris, France
    Neurosignals 11:130-43. 2002
  4. ncbi request reprint The C-terminal T peptide of cholinesterases: structure, interactions, and influence on protein folding and secretion
    Jean Massoulié
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, CNRS UMR8544, Ecole Normale Superieure, Paris, France
    J Mol Neurosci 30:233-6. 2006
  5. ncbi request reprint The C-terminal peptides of acetylcholinesterase: cellular trafficking, oligomerization and functional anchoring
    Jean Massoulié
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, 75005 Paris, France
    Chem Biol Interact 157:3-14. 2005
  6. pmc Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA
    Hiba Noureddine
    Laboratoire de Neurobiologie, Centre National de la Recherche Scientifique, UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, Paris, France
    J Biol Chem 283:20722-32. 2008
  7. doi request reprint Protein CutA undergoes an unusual transfer into the secretory pathway and affects the folding, oligomerization, and secretion of acetylcholinesterase
    Dong Liang
    Laboratoire de Neurobiologie, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, 75005 Paris, France
    J Biol Chem 284:5195-207. 2009
  8. ncbi request reprint The readthrough variant of acetylcholinesterase remains very minor after heat shock, organophosphate inhibition and stress, in cell culture and in vivo
    Noël A Perrier
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, Ecole Normale Superieure, Paris, France
    J Neurochem 94:629-38. 2005
  9. doi request reprint Unusual transfer of CutA into the secretory pathway, evidenced by fusion proteins with acetylcholinesterase
    Dong Liang
    Laboratoire de Neurobiologie, CNRS UMR 8544, Paris, France
    FEBS J 276:4473-82. 2009
  10. pmc The C-terminal T peptide of acetylcholinesterase enhances degradation of unassembled active subunits through the ERAD pathway
    Stéphanie Belbeoc'h
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, 75230 Paris Cedex 05, France
    EMBO J 22:3536-45. 2003

Collaborators

Detail Information

Publications15

  1. doi request reprint Old and new questions about cholinesterases
    Jean Massoulié
    Laboratoire de Neurobiologie, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, Paris, France
    Chem Biol Interact 175:30-44. 2008
    ..In addition, a number of provocative ideas concerning their proposed non-conventional, or non-catalytic functions deserve to be further documented...
  2. doi request reprint Cholinesterases and the basal lamina at vertebrate neuromuscular junctions
    Jean Massoulié
    Laboratoire de Neurobiologie, UMR8544 CNRS, Ecole Normale Superieure, 46 rue d Ulm, 75005 Paris, France
    Curr Opin Pharmacol 9:316-25. 2009
    ..Concurrent advances in understanding of the biological effects of specific ColQ-AChE mutations prefigure improved diagnostics and clinical approaches for some congenital myasthenic syndromes...
  3. ncbi request reprint The origin of the molecular diversity and functional anchoring of cholinesterases
    Jean Massoulié
    CNRS UMR 8544, Laboratoire de Neurobiologie, Ecole Normale Superieure, Paris, France
    Neurosignals 11:130-43. 2002
    ..In brain and muscles, the hydrolysis of acetylcholine by cholinesterases, in different contexts, and their possible noncatalytic functions clearly depend on their localization by ColQ or PRiMA...
  4. ncbi request reprint The C-terminal T peptide of cholinesterases: structure, interactions, and influence on protein folding and secretion
    Jean Massoulié
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, CNRS UMR8544, Ecole Normale Superieure, Paris, France
    J Mol Neurosci 30:233-6. 2006
    ..When reduced to their catalytic domain, AChE subunits without a t peptide are active but remain monomeric and soluble...
  5. ncbi request reprint The C-terminal peptides of acetylcholinesterase: cellular trafficking, oligomerization and functional anchoring
    Jean Massoulié
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, 75005 Paris, France
    Chem Biol Interact 157:3-14. 2005
    ....
  6. pmc Acetylcholinesterase associates differently with its anchoring proteins ColQ and PRiMA
    Hiba Noureddine
    Laboratoire de Neurobiologie, Centre National de la Recherche Scientifique, UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, Paris, France
    J Biol Chem 283:20722-32. 2008
    ..Complexes with PQ or with PRiMA contained heavy components, which migrated abnormally in SDS-PAGE but probably resulted from disulfide bonding of four AChE(T) subunits with the four upstream cysteines of the associated protein...
  7. doi request reprint Protein CutA undergoes an unusual transfer into the secretory pathway and affects the folding, oligomerization, and secretion of acetylcholinesterase
    Dong Liang
    Laboratoire de Neurobiologie, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, 75005 Paris, France
    J Biol Chem 284:5195-207. 2009
    ..We found no evidence for a direct interaction between CutA and AChE. The longer CutA variant seems to affect the processing and trafficking of secretory proteins, whereas the shorter one may have a distinct function in the cytoplasm...
  8. ncbi request reprint The readthrough variant of acetylcholinesterase remains very minor after heat shock, organophosphate inhibition and stress, in cell culture and in vivo
    Noël A Perrier
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, Ecole Normale Superieure, Paris, France
    J Neurochem 94:629-38. 2005
    ..We observed a moderate increase of the AChE(R) transcript in some cases, both in the mouse brain and in neuroblastoma cultures, but we did not detect any increase of the corresponding active enzyme...
  9. doi request reprint Unusual transfer of CutA into the secretory pathway, evidenced by fusion proteins with acetylcholinesterase
    Dong Liang
    Laboratoire de Neurobiologie, CNRS UMR 8544, Paris, France
    FEBS J 276:4473-82. 2009
    ..These experiments illustrate the value of using AChE as a reporter and reveals an unusual protein trafficking and secretory process...
  10. pmc The C-terminal T peptide of acetylcholinesterase enhances degradation of unassembled active subunits through the ERAD pathway
    Stéphanie Belbeoc'h
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, 75230 Paris Cedex 05, France
    EMBO J 22:3536-45. 2003
    ..This system appears particularly well suited to analyze the mechanisms which determine the degradation of correctly folded multidomain proteins in the ER...
  11. doi request reprint Respective roles of the catalytic domains and C-terminal tail peptides in the oligomerization and secretory trafficking of human acetylcholinesterase and butyrylcholinesterase
    Dong Liang
    Laboratoire de Neurobiologie, CNRS UMR 8544, Ecole Normale Superieure, Paris, France
    FEBS J 276:94-108. 2009
    ..Sequence comparisons show that the differences between the t peptides of AChE and BChE are remarkably conserved among all vertebrates, suggesting that they reflect distinct functional adaptations...
  12. ncbi request reprint Assembly of acetylcholinesterase tetramers by peptidic motifs from the proline-rich membrane anchor, PRiMA: competition between degradation and secretion pathways of heteromeric complexes
    Hiba Noureddine
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, 75005 Paris
    J Biol Chem 282:3487-97. 2007
    ..Interestingly, short PRiMA mutants, truncated within the proline-rich motif, reduced both cellular and secreted AChE activity, suggesting that their interaction with AChE(T) subunits induces their intracellular degradation...
  13. ncbi request reprint Expression of PRiMA in the mouse brain: membrane anchoring and accumulation of 'tailed' acetylcholinesterase
    Noël A Perrier
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, 75230 Paris Cedex 05, France
    Eur J Neurosci 18:1837-47. 2003
    ..We also show that, in both mouse and human, PRiMA proteins exist as two alternative splice variants which differ in their cytoplasmic regions...
  14. ncbi request reprint PRiMA: the membrane anchor of acetylcholinesterase in the brain
    Anselme L Perrier
    Laboratoire de Neurobiologie Cellulaire et Moleculaire, CNRS UMR 8544, Ecole Normale Superieure, 46 rue d Ulm, 75230 Paris Cedex 05, France
    Neuron 33:275-85. 2002
    ..Furthermore, we demonstrate that AChE is actually anchored in neural cell membranes through its interaction with PRiMA. Finally, we propose that only PRiMA anchors AChE in mammalian brain and muscle cell membranes...
  15. ncbi request reprint Non-antisense cellular responses to oligonucleotides
    Alain Anselmet
    CNRS UMR 8544, Laboratoire de Neurobiologie, Ecole Normale Superieure, Paris, France
    FEBS Lett 510:175-80. 2002
    ..In addition, a subset of oligonucleotides induced platelet aggregation, probably through their interaction with membrane receptors. Recognition of these effects is important for the design and interpretation of antisense experiments...