dc.contributor.author |
Cornes, Eric |
dc.contributor.author |
Porta-De-La-Riva, Montserrat |
dc.contributor.author |
Aristizábal-Corrales, David |
dc.contributor.author |
Brokate-Llanos, Ana María |
dc.contributor.author |
García-Rodríguez, Francisco Javier |
dc.contributor.author |
Ertl, Iris |
dc.contributor.author |
Díaz, Mònica |
dc.contributor.author |
Fontrodona Montals, Laura |
dc.contributor.author |
Reis, Kadri |
dc.contributor.author |
Johnsen, Robert |
dc.contributor.author |
Baillie, David |
dc.contributor.author |
Muñoz, Manuel J. |
dc.contributor.author |
Sarov, Mihail |
dc.contributor.author |
Dupuy, Denis |
dc.contributor.author |
Cerón, Julián |
dc.contributor.author |
Universitat Autònoma de Barcelona |
dc.date |
2015 |
dc.identifier |
https://ddd.uab.cat/record/256116 |
dc.identifier |
urn:10.1261/rna.052324.115 |
dc.identifier |
urn:oai:ddd.uab.cat:256116 |
dc.identifier |
urn:pmcid:PMC4536316 |
dc.identifier |
urn:pmc-uid:4536316 |
dc.identifier |
urn:pmid:26150554 |
dc.identifier |
urn:oai:pubmedcentral.nih.gov:4536316 |
dc.identifier |
urn:articleid:14699001v21p1544 |
dc.identifier |
urn:oai:egreta.uab.cat:publications/54a0f025-2ea7-4565-8236-fe912eb572a3 |
dc.identifier |
urn:scopus_id:84939839840 |
dc.format |
application/pdf |
dc.language |
eng |
dc.publisher |
|
dc.relation |
Instituto de Salud Carlos III PI12/01554 |
dc.relation |
RNA ; Vol. 21 (september 2015), p. 1544-1553 |
dc.rights |
open access |
dc.rights |
Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. |
dc.rights |
https://creativecommons.org/licenses/by-nc/4.0/ |
dc.subject |
Caenorhabditis elegans |
dc.subject |
Stress response |
dc.subject |
LSM, daf-16 |
dc.subject |
P bodies |
dc.subject |
Stress granules |
dc.title |
Cytoplasmic LSM-1 protein regulates stress responses through the insulin/IGF-1 signaling pathway in Caenorhabditis elegans |
dc.type |
Article |
dc.description.abstract |
Genes coding for members of the Sm-like (LSm) protein family are conserved through evolution from prokaryotes to humans. These proteins have been described as forming homo- or heterocomplexes implicated in a broad range of RNA-related functions. To date, the nuclear LSm2-8 and the cytoplasmic LSm1-7 heteroheptamers are the best characterized complexes in eukaryotes. Through a comprehensive functional study of the LSm family members, we found that lsm-1 and lsm-3 are not essential for C. elegans viability, but their perturbation, by RNAi or mutations, produces defects in development, reproduction, and motility. We further investigated the function of lsm-1, which encodes the distinctive protein of the cytoplasmic complex. RNA-seq analysis of lsm-1 mutants suggests that they have impaired Insulin/IGF-1 signaling (IIS), which is conserved in metazoans and involved in the response to various types of stress through the action of the FOXO transcription factor DAF-16. Further analysis using a DAF-16::GFP reporter indicated that heat stress-induced translocation of DAF-16 to the nuclei is dependent on lsm-1. Consistent with this, we observed that lsm-1 mutants display heightened sensitivity to thermal stress and starvation, while overexpression of lsm-1 has the opposite effect. We also observed that under stress, cytoplasmic LSm proteins aggregate into granules in an LSM-1-dependent manner. Moreover, we found that lsm-1 and lsm-3 are required for other processes regulated by the IIS pathway, such as aging and pathogen resistance. |