Synaptic control of mRNA translation by reversible assembly of XRN1 bodies
Repression of mRNA translation is linked to the formation of specific cytosolic foci such as stress granules and processing bodies, which store or degrade mRNAs. In neurons, synaptic activity regulates translation at the post-synapse and this is important for plasticity. N-methyl-D-aspartate (NMDA)...
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todo:paper_00219533_v128_n8_p1542_Luchelli2023-10-03T14:23:35Z Synaptic control of mRNA translation by reversible assembly of XRN1 bodies Luchelli, L. Thomas, M.G. Boccaccio, G.L. P body RNA granule Stress granule Synapse XRN1 exoribonuclease messenger RNA metabotropic receptor n methyl dextro aspartic acid synapsin unclassified drug XRN1 protein DNA binding protein exoribonuclease messenger RNA metabotropic receptor n methyl dextro aspartic acid receptor Xrn1 protein, mouse animal experiment animal tissue Article cell body cellular distribution controlled study dendrite dendritic spine hippocampal CA1 region hippocampal CA3 region hippocampal neuronal culture immunofluorescence nonhuman priority journal protein localization protein processing protein synthesis rat RNA translation synapse Western blotting amino acid sequence animal cell culture cell organelle gene expression regulation genetics metabolism molecular genetics mouse nerve cell Sprague Dawley rat synapse Amino Acid Sequence Animals Cells, Cultured DNA-Binding Proteins Exoribonucleases Gene Expression Regulation Mice Molecular Sequence Data Neurons Organelles Protein Biosynthesis Rats, Sprague-Dawley Receptors, Metabotropic Glutamate Receptors, N-Methyl-D-Aspartate RNA, Messenger Synapses Repression of mRNA translation is linked to the formation of specific cytosolic foci such as stress granules and processing bodies, which store or degrade mRNAs. In neurons, synaptic activity regulates translation at the post-synapse and this is important for plasticity. N-methyl-D-aspartate (NMDA) receptor stimulation downregulates translation, and we speculate that this is linked to the formation of unknown mRNA-silencing foci. Here, we show that the 5'-3' exoribonuclease XRN1 forms discrete clusters associated with the post-synapse that are different from processing bodies or stress granules, and we named them synaptic XRN1 bodies (SX-bodies). Using primary neurons, we found that the SX-bodies respond to synapse stimulation and that their formation correlates inversely with the local translation rate. SX-bodies increase in size and number upon NMDA stimulation, and metabotropic glutamate receptor activation provokes SX-body dissolution, along with increased translation. The response is specific and the previously described Smaug1 foci and FMRP granules show a different response. Finally, XRN1 knockdown impairs the translational repression triggered by NMDA. Collectively, these observations support a role for the SX-bodies in the reversible masking and silencing of mRNAs at the synapse. © 2015. Published by The Company of Biologists Ltd. Fil:Luchelli, L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Thomas, M.G. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Boccaccio, G.L. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00219533_v128_n8_p1542_Luchelli |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
P body RNA granule Stress granule Synapse XRN1 exoribonuclease messenger RNA metabotropic receptor n methyl dextro aspartic acid synapsin unclassified drug XRN1 protein DNA binding protein exoribonuclease messenger RNA metabotropic receptor n methyl dextro aspartic acid receptor Xrn1 protein, mouse animal experiment animal tissue Article cell body cellular distribution controlled study dendrite dendritic spine hippocampal CA1 region hippocampal CA3 region hippocampal neuronal culture immunofluorescence nonhuman priority journal protein localization protein processing protein synthesis rat RNA translation synapse Western blotting amino acid sequence animal cell culture cell organelle gene expression regulation genetics metabolism molecular genetics mouse nerve cell Sprague Dawley rat synapse Amino Acid Sequence Animals Cells, Cultured DNA-Binding Proteins Exoribonucleases Gene Expression Regulation Mice Molecular Sequence Data Neurons Organelles Protein Biosynthesis Rats, Sprague-Dawley Receptors, Metabotropic Glutamate Receptors, N-Methyl-D-Aspartate RNA, Messenger Synapses |
| spellingShingle |
P body RNA granule Stress granule Synapse XRN1 exoribonuclease messenger RNA metabotropic receptor n methyl dextro aspartic acid synapsin unclassified drug XRN1 protein DNA binding protein exoribonuclease messenger RNA metabotropic receptor n methyl dextro aspartic acid receptor Xrn1 protein, mouse animal experiment animal tissue Article cell body cellular distribution controlled study dendrite dendritic spine hippocampal CA1 region hippocampal CA3 region hippocampal neuronal culture immunofluorescence nonhuman priority journal protein localization protein processing protein synthesis rat RNA translation synapse Western blotting amino acid sequence animal cell culture cell organelle gene expression regulation genetics metabolism molecular genetics mouse nerve cell Sprague Dawley rat synapse Amino Acid Sequence Animals Cells, Cultured DNA-Binding Proteins Exoribonucleases Gene Expression Regulation Mice Molecular Sequence Data Neurons Organelles Protein Biosynthesis Rats, Sprague-Dawley Receptors, Metabotropic Glutamate Receptors, N-Methyl-D-Aspartate RNA, Messenger Synapses Luchelli, L. Thomas, M.G. Boccaccio, G.L. Synaptic control of mRNA translation by reversible assembly of XRN1 bodies |
| topic_facet |
P body RNA granule Stress granule Synapse XRN1 exoribonuclease messenger RNA metabotropic receptor n methyl dextro aspartic acid synapsin unclassified drug XRN1 protein DNA binding protein exoribonuclease messenger RNA metabotropic receptor n methyl dextro aspartic acid receptor Xrn1 protein, mouse animal experiment animal tissue Article cell body cellular distribution controlled study dendrite dendritic spine hippocampal CA1 region hippocampal CA3 region hippocampal neuronal culture immunofluorescence nonhuman priority journal protein localization protein processing protein synthesis rat RNA translation synapse Western blotting amino acid sequence animal cell culture cell organelle gene expression regulation genetics metabolism molecular genetics mouse nerve cell Sprague Dawley rat synapse Amino Acid Sequence Animals Cells, Cultured DNA-Binding Proteins Exoribonucleases Gene Expression Regulation Mice Molecular Sequence Data Neurons Organelles Protein Biosynthesis Rats, Sprague-Dawley Receptors, Metabotropic Glutamate Receptors, N-Methyl-D-Aspartate RNA, Messenger Synapses |
| description |
Repression of mRNA translation is linked to the formation of specific cytosolic foci such as stress granules and processing bodies, which store or degrade mRNAs. In neurons, synaptic activity regulates translation at the post-synapse and this is important for plasticity. N-methyl-D-aspartate (NMDA) receptor stimulation downregulates translation, and we speculate that this is linked to the formation of unknown mRNA-silencing foci. Here, we show that the 5'-3' exoribonuclease XRN1 forms discrete clusters associated with the post-synapse that are different from processing bodies or stress granules, and we named them synaptic XRN1 bodies (SX-bodies). Using primary neurons, we found that the SX-bodies respond to synapse stimulation and that their formation correlates inversely with the local translation rate. SX-bodies increase in size and number upon NMDA stimulation, and metabotropic glutamate receptor activation provokes SX-body dissolution, along with increased translation. The response is specific and the previously described Smaug1 foci and FMRP granules show a different response. Finally, XRN1 knockdown impairs the translational repression triggered by NMDA. Collectively, these observations support a role for the SX-bodies in the reversible masking and silencing of mRNAs at the synapse. © 2015. Published by The Company of Biologists Ltd. |
| format |
JOUR |
| author |
Luchelli, L. Thomas, M.G. Boccaccio, G.L. |
| author_facet |
Luchelli, L. Thomas, M.G. Boccaccio, G.L. |
| author_sort |
Luchelli, L. |
| title |
Synaptic control of mRNA translation by reversible assembly of XRN1 bodies |
| title_short |
Synaptic control of mRNA translation by reversible assembly of XRN1 bodies |
| title_full |
Synaptic control of mRNA translation by reversible assembly of XRN1 bodies |
| title_fullStr |
Synaptic control of mRNA translation by reversible assembly of XRN1 bodies |
| title_full_unstemmed |
Synaptic control of mRNA translation by reversible assembly of XRN1 bodies |
| title_sort |
synaptic control of mrna translation by reversible assembly of xrn1 bodies |
| url |
http://hdl.handle.net/20.500.12110/paper_00219533_v128_n8_p1542_Luchelli |
| work_keys_str_mv |
AT luchellil synapticcontrolofmrnatranslationbyreversibleassemblyofxrn1bodies AT thomasmg synapticcontrolofmrnatranslationbyreversibleassemblyofxrn1bodies AT boccacciogl synapticcontrolofmrnatranslationbyreversibleassemblyofxrn1bodies |
| _version_ |
1782023485259776000 |