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TitleA J-domain protein enhances memory by promoting physiological amyloid formation in .
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 123, Issue 5, Page e2516310123, Year 2026
Publish dateFeb 3, 2026
AuthorsKyle Patton / Yangyang Yi / Raj Burt / Kevin Kan-Shing Ng / Mayur Mukhi / Peerzada Shariq Shaheen Khaki / Ruben Hervas / Kausik Si /
PubMed AbstractMemory requires experience-dependent alterations in the synaptic proteome. Chaperones interface between the environment and the proteome. Manipulating J-domain protein (JDP) chaperones, the most ...Memory requires experience-dependent alterations in the synaptic proteome. Chaperones interface between the environment and the proteome. Manipulating J-domain protein (JDP) chaperones, the most diverse family of chaperones, in a neuronal circuit that encodes associative long-term memories, we identified yet uncharacterized JDPs that transduce sensory cues. One of these JDPs, CG10375, which we named Funes, enhances memory when overexpressed and impairs memory when functionally impaired. Funes overexpression enhances memory formation even when sensory stimuli are suboptimal. At the circuit level, Funes acts on neurons where conditioned and unconditioned stimuli converge to form associative memories. From a proteomic-based screen, we found that overexpression of Funes changes the solubility of a small subset of proteins, one of which is the mRNA-binding protein Orb2. Combining in vitro and in vivo biophysical, biochemical, and cryo-EM structural analyses, we found that Funes associates with oligomeric Orb2 and promotes the formation of translationally active amyloids. Perturbation of the conserved J domain eliminates the ability of Funes to facilitate amyloid assembly and promote memory. We posit that the brain harbors chaperones that influence memory by regulating physiological amyloid formation.
External linksProc Natl Acad Sci U S A / PubMed:41615743 / PubMed Central
MethodsEM (helical sym.)
Resolution3.1 Å
Structure data

39095

8yac

EMDB-39095, PDB-8yac:
Funes-induced Orb2 amyloid like endogenous Orb2 amyloid
Method: EM (helical sym.) / Resolution: 3.1 Å

Source
  • drosophila melanogaster (fruit fly)
KeywordsPROTEIN FIBRIL / Translator regulator / chaperone

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