| http://purl.uniprot.org/citations/32467239 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/32467239 | http://www.w3.org/2000/01/rdf-schema#comment | "Molecular chaperones often work collaboratively with the ubiquitylation-proteasome system (UPS) to facilitate the degradation of misfolded proteins, which typically safeguards cellular differentiation and protects cells from stress. In this study, however, we report that the Hsp70/Hsp90 chaperone machinery and an F-box protein, MEC-15, have opposing effects on neuronal differentiation, and that the chaperones negatively regulate neuronal morphogenesis and functions. Using the touch receptor neurons (TRNs) of Caenorhabditis elegans, we find that mec-15(-) mutants display defects in microtubule formation, neurite growth, synaptic development and neuronal functions, and that these defects can be rescued by the loss of Hsp70/Hsp90 chaperones and co-chaperones. MEC-15 probably functions in a Skp-, Cullin- and F-box-containing complex to degrade DLK-1, which is an Hsp90 client protein stabilized by the chaperones. The abundance of DLK-1, and likely other Hsp90 substrates, is fine-tuned by the antagonism between MEC-15 and the chaperones; this antagonism regulates TRN development, as well as synaptic functions of GABAergic motor neurons. Therefore, a balance between the UPS and the chaperones tightly controls neuronal differentiation."xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.org/dc/terms/identifier | "doi:10.1242/dev.189886"xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/author | "Zheng C."xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/author | "Hall D.H."xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/author | "Chalfie M."xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/author | "Nguyen K.C.Q."xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/author | "Atlas E."xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/author | "Jao S.L.J."xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/author | "Lee H.M.T."xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/date | "2020"xsd:gYear |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/name | "Development"xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/pages | "dev189886"xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/title | "Opposing effects of an F-box protein and the HSP90 chaperone network on microtubule stability and neurite growth in Caenorhabditis elegans."xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://purl.uniprot.org/core/volume | "147"xsd:string |
| http://purl.uniprot.org/citations/32467239 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/32467239 |
| http://purl.uniprot.org/citations/32467239 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/32467239 |
| http://purl.uniprot.org/uniprot/#_Q18688-mappedCitation-32467239 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/32467239 |
| http://purl.uniprot.org/uniprot/#_Q22071-mappedCitation-32467239 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/32467239 |
| http://purl.uniprot.org/uniprot/Q22071 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/32467239 |
| http://purl.uniprot.org/uniprot/Q18688 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/32467239 |