{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Alecki C"],"funding":["ALS Society of Canada (ALS Canada)","NIMH NIH HHS","NHGRI NIH HHS","NCI NIH HHS","NINDS NIH HHS","U.S. Department of Health & Human Services | National Institutes of Health (NIH)","Fonds de Recherche du Québec - Santé (Fonds de la recherche en sante du Quebec)","Gouvernement du Canada | Canadian Institutes of Health Research (Instituts de Recherche en Santé du Canada)"],"pagination":["10796"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11685665"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Proteostasis is maintained through regulated protein synthesis and degradation and chaperone-assisted protein folding. However, this is challenging in neuronal projections because of their polarized morphology and constant synaptic proteome remodeling. Using high-resolution fluorescence microscopy, we discover that hippocampal and spinal cord motor neurons of mouse and human origin localize a subset of chaperone mRNAs to their dendrites and use microtubule-based transport to increase this asymmetric localization following proteotoxic stress. The most abundant dendritic chaperone mRNA encodes a constitutive heat shock protein 70 family member (HSPA8). Proteotoxic stress also enhances HSPA8 mRNA translation efficiency in dendrites. Stress-mediated HSPA8 mRNA localization to the dendrites is "],"journal":["Nature communications"],"pubmed_title":["Localized molecular chaperone synthesis maintains neuronal dendrite proteostasis."],"pmcid":["PMC11685665"],"funding_grant_id":["HG011864","P30 CA008748","HG009889","2022-ALS Discovery Grant","R01 HG004659","U41 HG009889","PJT-186141","HG004659","R01 HG011864","R01 NS103172","RF1 MH126719","MH126719","300232","Hudson Translational Team Grant","U24 HG009889"],"pubmed_authors":["Lynch J","Verbrugghe M","Alecki C","Xu JMS","Jacob-Tomas S","Yeo GW","Le P","Vera M","Comaduran MF","Rizwan J","Biswas J","Durham HD","Wu T","Minotti S"],"additional_accession":[]},"is_claimable":false,"name":"Localized molecular chaperone synthesis maintains neuronal dendrite proteostasis.","description":"Proteostasis is maintained through regulated protein synthesis and degradation and chaperone-assisted protein folding. However, this is challenging in neuronal projections because of their polarized morphology and constant synaptic proteome remodeling. Using high-resolution fluorescence microscopy, we discover that hippocampal and spinal cord motor neurons of mouse and human origin localize a subset of chaperone mRNAs to their dendrites and use microtubule-based transport to increase this asymmetric localization following proteotoxic stress. The most abundant dendritic chaperone mRNA encodes a constitutive heat shock protein 70 family member (HSPA8). Proteotoxic stress also enhances HSPA8 mRNA translation efficiency in dendrites. Stress-mediated HSPA8 mRNA localization to the dendrites is ","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Dec","modification":"2026-06-02T07:28:03.351Z","creation":"2025-04-05T17:01:11.283Z"},"accession":"S-EPMC11685665","cross_references":{"pubmed":["39737952"],"doi":["10.1038/s41467-024-55055-7"]}}