Falcon deep research report for DNAJB2
Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Human homologues of the bacterial heat-shock protein DnaJ are preferentially expressed in neurons.
The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities.
Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3.
The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation.
Molecular chaperone mediated late-stage neuroprotection in the SOD1(G93A) mouse model of amyotrophic lateral sclerosis.
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.
Protein kinase CK2 modulates HSJ1 function through phosphorylation of the UIM2 domain.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Regulation of 70-kDa heat-shock-protein ATPase activity and substrate binding by human DnaJ-like proteins, HSJ1a and HSJ1b.
Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70.
Neuromuscular diseases due to chaperone mutations - a review and some new results.
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DNAJB2 cooperates with CHIP/STUB1-mediated ubiquitylation and protects polyubiquitin chains from deubiquitylation, supporting a shuttle/stabilization role for ubiquitinated clients destined for proteasomal degradation.
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CK2 phosphorylation of UIM2 reduces HSJ1's ability to bind ubiquitylated clients, providing a kinase-dependent regulatory mechanism for DNAJB2 proteostasis functions.
Extension of the DNAJB2a isoform in a dominant neuromyopathy family.
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First dominantly acting DNAJB2 mutation reported: stop-loss variant (p.*278Glyext*83) creates a transmembrane helix driving ER mislocalization and proteasomal degradation of mutant DNAJB2a with dominant-negative effects on wild-type protein.
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Approximately 50% reduction of both DNAJB2 isoforms in patient muscle tissue, with rapid cycloheximide-chase turnover of the extension mutant rescued by MG132 proteasome inhibition.
Current advance on distal myopathy genetics.
J protein mutations and resulting proteostasis collapse.
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DNAJB2 is an anti-aggregation cochaperone suppressing aggregation of diverse neurodegeneration-associated proteins including polyQ-expanded huntingtin, parkin, SOD1, and TDP-43.
Impaired DNAJB2 response to heat shock in fibroblasts from a neuropathy patient with DNAJB2/HSJ1 mutation - cystamine as a potential therapeutic intervention.