Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
The Caenorhabditis elegans hsp70 gene family: a molecular genetic characterization.
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Characterized hsp70 gene family in C. elegans
"We have isolated genomic clones representing six distinct members of the Caenorhabditis elegans 70-kDa heat-shock protein gene (hsp70) family."
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hsp70A (hsp-1) is constitutively expressed and also heat-inducible (2-6 fold)
"Transcripts of another gene, hsp70A, are abundant in control worms and are also increased (two- to six-fold) upon heat shock."
Regulation of longevity in Caenorhabditis elegans by heat shock factor and molecular chaperones.
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HSF-1 regulates longevity through molecular chaperone targets
"Down-regulation of hsf-1 by RNA interference suppressed longevity of mutants in an insulin-like signaling (ILS) pathway"
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Down-regulation of individual chaperones decreases longevity in long-lived ILS mutants
"Down-regulation of individual molecular chaperones, transcriptional targets of HSF-1, also decreased longevity of long-lived mutant but not wild-type animals."
Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans.
Knockdown of mitochondrial heat shock protein 70 promotes progeria-like phenotypes in caenorhabditis elegans.
C. elegans STI-1, the homolog of Sti1/Hop, is involved in aging and stress response.
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STI-1 binds both Hsp70 and Hsp90 homologs
"Analysis of proteins immunoprecipitated with anti-STI-1 antibody by mass spectrometry revealed that CeSTI-1 can bind with both Hsp70 and Hsp90 homologs like its mammalian counterpart."
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STI-1 functions in thermotolerance and longevity
"sti-1(jh125) mutants have a shortened life span."
The non-canonical Hop protein from Caenorhabditis elegans exerts essential functions and forms binary complexes with either Hsc70 or Hsp90.
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CeHop forms binary complexes with Hsc70
"Interestingly, we observed physical interactions with both chaperones Hsp70 and Hsp90, albeit only the interaction with Hsp90 is strong"
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Demonstrated ATPase activity interaction
"inhibition of the Hsp90 ATPase activity can be observed upon binding of CeHop"
Regulation of endosomal clathrin and retromer-mediated endosome to Golgi retrograde transport by the J-domain protein RME-8.
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HSP-1 functions with RME-8 in endosomal trafficking
"retromer can regulate endosomal clathrin dynamics through RME-8 and Hsc70"
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Loss of HSP-1 causes endosomal clathrin accumulation
"Loss of SNX-1, RME-8, or the clathrin chaperone Hsc70/HSP-1 leads to over-accumulation of endosomal clathrin, reduced clathrin dynamics, and missorting of MIG-14 to the lysosome."
Regulation of DAF-16-mediated Innate Immunity in Caenorhabditis elegans.
The myosin chaperone UNC-45 is organized in tandem modules to support myofilament formation in C. elegans.
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UNC-45 interacts with Hsp70 via TPR domain
"Accordingly, Hsp70 and Hsp90, which bind to the TPR domain of UNC-45, could act in concert and with defined periodicity on captured myosin molecules."
The balanced regulation of Hsc70 by DNJ-13 and UNC-23 is required for muscle functionality.
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Demonstrated HSP-1 ATPase activity biochemically
"C-terminal fragments of UNC-23 instead perform all Hsc70-related functions, like ATPase stimulation and regulation of folding activity, albeit with lower affinity than BAG-1."
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DNJ-13 and UNC-23 regulate Hsc70 ATPase cycle antagonistically
"the motility dysfunction in the unc-23 mutated strain can be cured specifically by down-regulation of the antagonistic Hsc70 cochaperone DNJ-13"
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Balanced regulation essential for muscle function
"the balanced action of cofactors in the ATP-driven cycle of Hsc70 is crucial for the contribution of Hsc70 to muscle functionality."
The C. elegans UNC-23 protein, a member of the BCL-2-associated athanogene (BAG) family of chaperone regulators, interacts with HSP-1 to regulate cell attachment and maintain hypodermal integrity.
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UNC-23 binds HSP-1 ATPase domain
"We have isolated missense mutations in the ATPase domain of the C. elegans heat shock 70 protein, HSP-1 that suppress the phenotype exhibited by unc-23(e25) mutant hermaphrodites"
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Yeast two-hybrid confirmation of interaction
"we show that UNC-23 and HSP-1 interact in a yeast-2-hybrid system."
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HSP-1/UNC-23 required for muscle attachment
"The interaction of UNC-23 with HSP-1 defines a role for HSP-1 function in the maintenance of muscle attachment during development."
The Caenorhabditis elegans protein FIC-1 is an AMPylase that covalently modifies heat-shock 70 family proteins, translation elongation factors and histones.
Visible light reduces C. elegans longevity.
Caenorhabditis elegans auxilin: a J-domain protein essential for clathrin-mediated endocytosis in vivo.
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Hsc70 uncoats clathrin-coated vesicles in an ATP-dependent, J-domain (auxilin)-dependent reaction; C. elegans has a single auxilin (dnj-25) whose in vitro activity matches mammalian auxilin.
"In vitro, the molecular chaperone Hsc70 uncoats clathrin-coated vesicles in an ATP-dependent process that requires a specific J-domain protein such as auxilin."
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Loss of the worm auxilin disrupts clathrin distribution and dynamics in vivo, consistent with a conserved Hsc70/auxilin uncoating reaction.
"most of these worms arrest during larval development, exhibit defective distribution of GFP-clathrin in many cell types, and show a marked change in clathrin dynamics"
Deep research report on hsp-1