Interactions of S100A2 and S100A6 with the Tetratricopeptide Repeat Proteins, Hsp90/Hsp70-organizing Protein and Kinesin Light Chain*

@article{Shimamoto2008InteractionsOS,
  title={Interactions of S100A2 and S100A6 with the Tetratricopeptide Repeat Proteins, Hsp90/Hsp70-organizing Protein and Kinesin Light Chain*},
  author={Seiko Shimamoto and Maki Takata and Masaaki Tokuda and Fumikazu Oohira and Hiroshi Tokumitsu and Ryoji Kobayashi},
  journal={Journal of Biological Chemistry},
  year={2008},
  volume={283},
  pages={28246 - 28258}
}
S100A2 and S100A6 interact with several target proteins in a Ca2+-regulated manner. However, the exact intracellular roles of the S100 proteins are unclear. In this study we identified Hsp70/Hsp90-organizing protein (Hop) and kinesin light chain (KLC) as novel targets of S100A2 and S100A6. Hop directly associates with Hsp70 and Hsp90 through the tetratricopeptide (TPR) domains and regulates Hop-Hsp70 and Hop-Hsp90 complex formation. We have found that S100A2 and S100A6 bind to the TPR domain of… Expand
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References

SHOWING 1-10 OF 31 REFERENCES
S100A1 Is a Novel Molecular Chaperone and a Member of the Hsp70/Hsp90 Multichaperone Complex*
TLDR
The chaperone activity of S100A1 was antagonized by calmodulin antagonists, that is, indeed an intrinsic function of the protein, and bring us closer to a comprehensive understanding of the molecular mechanisms of the Hsp70/Hsp90 multichaperone complex. Expand
Identification of CHIP, a Novel Tetratricopeptide Repeat-Containing Protein That Interacts with Heat Shock Proteins and Negatively Regulates Chaperone Functions
TLDR
Results indicate that CHIP decreases net ATPase activity and reduces chaperone efficiency, and they implicate CHIP in the negative regulation of the forward reaction of the Hsc70-Hsp70 substrate-binding cycle. Expand
Multiple Domains of the Co-chaperone Hop Are Important for Hsp70 Binding*
TLDR
Surprisingly, truncation of EEVD plus as many as 34 additional amino acids from the Hsp70 C terminus did not reduce the ability of HSp70 mutants to co-immunoprecipitate with Hop, although further truncation eliminated Hop binding. Expand
Tetratricopeptide Repeat Motif-mediated Hsc70-mSTI1 Interaction
TLDR
It is proposed that the electrostatic interactions in the first TPR motif made by Lys8 or Asn12 define part of the minimum interactions required for successful mSTI1-Hsc70 interaction. Expand
Hop Modulates hsp70/hsp90 Interactions in Protein Folding*
TLDR
It is shown that Hop is involved in the process of refolding thermally denatured firefly luciferase in rabbit reticulocyte lysate and that Hop modulates the activities of both of these chaperone proteins. Expand
Regulation of Hsp90 ATPase activity by tetratricopeptide repeat (TPR)‐domain co‐chaperones
TLDR
An important role for TPR‐domain co‐chaperones as regulators of the ATPase activity of Hsp90 is revealed, showing that the ATP‐dependent step in HSp90‐mediated protein folding occurs after the binding of the folding client protein, and suggesting that ATP hydrolysis triggers client‐protein release. Expand
Hop as an Adaptor in the Heat Shock Protein 70 (Hsp70) and Hsp90 Chaperone Machinery*
TLDR
Hop has a novel role in the chaperone machinery as an adaptor that can integrate Hsp70 and Hsp90 interactions and is targeted for small substitutions and deletions. Expand
The Assembly and Intermolecular Properties of the hsp70-Hop-hsp90 Molecular Chaperone Complex*
TLDR
The results suggest that the assembly of hsp70-Hop-hsp90 complexes is selective and influences the conformational state of each protein. Expand
Interaction of S100 proteins with the antiallergic drugs, olopatadine, amlexanox, and cromolyn: identification of putative drug binding sites on S100A1 protein.
TLDR
Results indicate that C-terminal region of S100A1 is important for antiallergic drug binding, although the drug binding sites are different according to each anti allergic drug. Expand
Calcium-dependent and -independent interactions of the S100 protein family.
TLDR
This review highlights both the calcium-dependent and -independent interactions of the S100 proteins, with a focus on the structures of the complexes, differences and similarities in the strengths of the interactions, and preferences for homo- compared with hetero-dimeric S100 protein assembly. Expand
...
1
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3
4
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