Artikel ; Online: Mrj is a chaperone of the Hsp40 family that regulates Orb2 oligomerization and long-term memory in Drosophila.
2024 Band 22, Heft 4, Seite(n) e3002585
Abstract: Orb2 the Drosophila homolog of cytoplasmic polyadenylation element binding (CPEB) protein forms prion-like oligomers. These oligomers consist of Orb2A and Orb2B isoforms and their formation is dependent on the oligomerization of the Orb2A isoform. ... ...
Abstract | Orb2 the Drosophila homolog of cytoplasmic polyadenylation element binding (CPEB) protein forms prion-like oligomers. These oligomers consist of Orb2A and Orb2B isoforms and their formation is dependent on the oligomerization of the Orb2A isoform. Drosophila with a mutation diminishing Orb2A's prion-like oligomerization forms long-term memory but fails to maintain it over time. Since this prion-like oligomerization of Orb2A plays a crucial role in the maintenance of memory, here, we aim to find what regulates this oligomerization. In an immunoprecipitation-based screen, we identify interactors of Orb2A in the Hsp40 and Hsp70 families of proteins. Among these, we find an Hsp40 family protein Mrj as a regulator of the conversion of Orb2A to its prion-like form. Mrj interacts with Hsp70 proteins and acts as a chaperone by interfering with the aggregation of pathogenic Huntingtin. Unlike its mammalian homolog, we find Drosophila Mrj is neither an essential gene nor causes any gross neurodevelopmental defect. We observe a loss of Mrj results in a reduction in Orb2 oligomers. Further, Mrj knockout exhibits a deficit in long-term memory and our observations suggest Mrj is needed in mushroom body neurons for the regulation of long-term memory. Our work implicates a chaperone Mrj in mechanisms of memory regulation through controlling the oligomerization of Orb2A and its association with the translating ribosomes. |
---|---|
Mesh-Begriff(e) | Animals ; Drosophila melanogaster/metabolism ; Drosophila melanogaster/genetics ; Drosophila Proteins/metabolism ; Drosophila Proteins/genetics ; HSP40 Heat-Shock Proteins/metabolism ; HSP40 Heat-Shock Proteins/genetics ; HSP70 Heat-Shock Proteins/metabolism ; HSP70 Heat-Shock Proteins/genetics ; Memory, Long-Term/physiology ; mRNA Cleavage and Polyadenylation Factors/metabolism ; mRNA Cleavage and Polyadenylation Factors/genetics ; Mushroom Bodies/metabolism ; Protein Multimerization ; Transcription Factors/metabolism ; Transcription Factors/genetics ; Molecular Chaperones/genetics ; Molecular Chaperones/metabolism |
Chemische Substanzen | Drosophila Proteins ; HSP40 Heat-Shock Proteins ; HSP70 Heat-Shock Proteins ; mRNA Cleavage and Polyadenylation Factors ; Orb2 protein, Drosophila ; Transcription Factors ; mrj protein, Drosophila ; Molecular Chaperones |
Sprache | Englisch |
Erscheinungsdatum | 2024-04-22 |
Erscheinungsland | United States |
Dokumenttyp | Journal Article ; Research Support, Non-U.S. Gov't |
ZDB-ID | 2126776-5 |
ISSN | 1545-7885 ; 1544-9173 |
ISSN (online) | 1545-7885 |
ISSN | 1544-9173 |
DOI | 10.1371/journal.pbio.3002585 |
Datenquelle | MEDical Literature Analysis and Retrieval System OnLINE |
Zusatzmaterialien
Kategorien
Verfügbar in ZB MED Köln/Königswinter
Zs.A 6193: Hefte anzeigen | Standort: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG) |
Über subito bestellen
Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.