Poly(GR) interacts with key stress granule factors promoting its assembly into cytoplasmic inclusions.

Animals Mice Humans Amyotrophic Lateral Sclerosis / pathology DNA Helicases / metabolism Stress Granules DNA Repeat Expansion Poly-ADP-Ribose Binding Proteins / genetics RNA Helicases / genetics RNA Recognition Motif Proteins / metabolism Frontotemporal Dementia / metabolism Inclusion Bodies / metabolism Heat-Shock Proteins / metabolism RNA / metabolism C9orf72 Protein / genetics
CP: Molecular biology CP: Neuroscience G3BP1/2 YTHDF proteins amyotrophic lateral sclerosis chromosome 9 open reading frame 72 cytoplasmic poly(GR) inclusions dipeptide repeat proteins frontotemporal dementia liquid-liquid phase separation m6A-modified RNAs

Journal

Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691

Informations de publication

Date de publication:
29 08 2023
Historique:
received: 24 06 2022
revised: 14 12 2022
accepted: 01 07 2023
medline: 25 9 2023
pubmed: 20 7 2023
entrez: 20 7 2023
Statut: ppublish

Résumé

C9orf72 repeat expansions are the most common genetic cause of frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS). Poly(GR) proteins are toxic to neurons by forming cytoplasmic inclusions that sequester RNA-binding proteins including stress granule (SG) proteins. However, little is known of the factors governing poly(GR) inclusion formation. Here, we show that poly(GR) infiltrates a finely tuned network of protein-RNA interactions underpinning SG formation. It interacts with G3BP1, the key driver of SG assembly and a protein we found is critical for poly(GR) inclusion formation. Moreover, we discovered that N

Identifiants

DOI: 10.1016/j.celrep.2023.112822 PMID: 37471224 PMC: PMC10528326
pubmed: 37471224
pii: S2211-1247(23)00833-1
doi: 10.1016/j.celrep.2023.112822
pmc: PMC10528326
mid: NIHMS1928384
pii:
doi:

Substances chimiques

DNA Helicases EC 3.6.4.-
Poly-ADP-Ribose Binding Proteins 0
RNA Helicases EC 3.6.4.13
RNA Recognition Motif Proteins 0
Heat-Shock Proteins 0
RNA 63231-63-0
C9orf72 Protein 0
G3BP1 protein, human EC 3.6.4.12

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

112822

Subventions

Organisme : NINDS NIH HHS
ID : R35 NS097273
Pays : United States
Organisme : NIA NIH HHS
ID : RF1 AG062171
Pays : United States
Organisme : NIA NIH HHS
ID : RF1 AG062077
Pays : United States
Organisme : NINDS NIH HHS
ID : R21 NS127331
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS117461
Pays : United States
Organisme : NIA NIH HHS
ID : RF1 AG061706
Pays : United States
Organisme : NINDS NIH HHS
ID : P01 NS084974
Pays : United States
Organisme : NIA NIH HHS
ID : R01 AG080810
Pays : United States
Organisme : NINDS NIH HHS
ID : P01 NS099114
Pays : United States
Organisme : NINDS NIH HHS
ID : U54 NS123743
Pays : United States

Informations de copyright

Copyright © 2023 The Author(s). Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests.

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Auteurs

Jinyoung Park (J)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.

Yanwei Wu (Y)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.

Wei Shao (W)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.

Tania F Gendron (TF)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA; Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN 55902, USA.

Sophie J F van der Spek (SJF)

Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA 02118, USA.

Grigorii Sultanakhmetov (G)

Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA 02118, USA; Department of Biological Sciences, Graduate School of Science, Tokyo Metropolitan University, Tokyo, 1920397, Japan.

Avik Basu (A)

Center for Network Systems Biology, Boston University School of Medicine, Boston, MA 02118, USA.

Paula Castellanos Otero (P)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.

Caroline J Jones (CJ)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.

Karen Jansen-West (K)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.

Lillian M Daughrity (LM)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.

Sadhna Phanse (S)

Center for Network Systems Biology, Boston University School of Medicine, Boston, MA 02118, USA.

Giulia Del Rosso (G)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.

Jimei Tong (J)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.

Monica Castanedes-Casey (M)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA.

Lulu Jiang (L)

Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA 02118, USA.

Jenna Libera (J)

Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA 02118, USA.

Björn Oskarsson (B)

Department of Neurology, Mayo Clinic, Jacksonville, FL 32224, USA.

Dennis W Dickson (DW)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA; Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN 55902, USA.

David W Sanders (DW)

Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544, USA.

Clifford P Brangwynne (CP)

Department of Chemical and Biological Engineering, Princeton University, Princeton, NJ 08544, USA; Howard Hughes Medical Institute, Princeton, NJ 08544, USA.

Andrew Emili (A)

Center for Network Systems Biology, Boston University School of Medicine, Boston, MA 02118, USA.

Benjamin Wolozin (B)

Department of Pharmacology and Experimental Therapeutics, Boston University School of Medicine, Boston, MA 02118, USA.

Leonard Petrucelli (L)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA; Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN 55902, USA. Electronic address: petrucelli.leonard@mayo.edu.

Yong-Jie Zhang (YJ)

Department of Neuroscience, Mayo Clinic, Jacksonville, FL 32224, USA; Neurobiology of Disease Graduate Program, Mayo Graduate School, Mayo Clinic College of Medicine, Rochester, MN 55902, USA. Electronic address: zhang.yongjie@mayo.edu.

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Classifications MeSH

questionsmedicales.fr › Eucaryotes › Animaux › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Rodentia › Muridae › Murinae › Souris › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Maladies métaboliques et nutritionnelles › Maladies métaboliques › Troubles de l'homéostasie des protéines › Protéinopathies TDP-43 › Sclérose latérale amyotrophique › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Isomerases › Helicase › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Cellules › Structures cellulaires › Espace intracellulaire › Cytoplasme › Structures cytoplasmiques › Organites › Vésicules cytoplasmiques › Granulations cytoplasmiques › Granules ribonucléoprotéiques cytoplasmiques › Granules de stress › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Phénomènes génétiques › Mutagenèse › Expansion de séquence répétée de l'ADN › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines nucléaires › Protéines liant le poly-adp-ribose › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Transferases › Phosphotransferases › Nucleotidyltransferases › RNA nucleotidyltransferases › RNA helicases › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Nucléoprotéines › Protéines de liaison à l'ARN › Protéines à motif de reconnaissance de l'ARN › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Troubles mentaux › Troubles neurocognitifs › Démence › Dégénérescence lobaire frontotemporale › Démence frontotemporale › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Cellules › Structures cellulaires › Corps d'inclusion › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Chaperons moléculaires › Protéines du choc thermique › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Acides nucléiques, nucléotides et nucléosides › Acides nucléiques › ARN › Poly(GR) interacts with key stress granule...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Régulateurs des protéines G › Facteurs d'échange de nucléotides guanyliques › Protéine C9orf72 › Poly(GR) interacts with key stress granule...