ArticleThe Biochemical journal2001
Different combinations of the heat-shock cognate protein 70 (hsc70) C-terminal functional groups are utilized to interact with distinct tetratricopeptide repeat-containing proteins.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 69 citations in OpenAlex.
- SGTA associates with intracellular aggregates in neurodegenerative diseases.Molecular brain · 2021Article
- The Effect of Mutations in the TPR and Ankyrin Families of Alpha Solenoid Repeat Proteins.Frontiers in bioinformatics · 2021Review
- Hsc70/Stub1 promotes the removal of individual oxidatively stressed peroxisomes.Nature communications · 2020Article
- Targeting Hsp70 facilitated protein quality control for treatment of polyglutamine diseases.Cellular and molecular life sciences : CMLS · 2020Review
- Effects of abiotic stress on the expression of Hsp70 genes in Sogatella furcifera (Horváth).Cell stress & chaperones · 2020Article
- The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast.The Journal of biological chemistry · 2018Article
- SGTA-Dependent Regulation of Hsc70 Promotes Cytosol Entry of Simian Virus 40 from the Endoplasmic Reticulum.Journal of virology · 2017Article
- Article
- Molecular cloning and expression of two heat-shock protein genes (HSC70/HSP70) from Prenant's schizothoracin (Schizothorax prenanti).Fish physiology and biochemistry · 2015Article
- A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins.Structure (London, England : 1993) · 2015Article
- Spectroscopic and thermodynamic properties of recombinant heat shock protein A6 from Camelus dromedarius.European biophysics journal : EBJ · 2015Article
- Expression profiles of the heat shock protein 70 gene in response to heat stress in Agrotis c-nigrum (Lepidoptera: Noctuidae).Journal of insect science (Online) · 2015Article
- The cochaperone SGTA (small glutamine-rich tetratricopeptide repeat-containing protein alpha) demonstrates regulatory specificity for the androgen, glucocorticoid, and progesterone receptors.The Journal of biological chemistry · 2014Article
- The molecular chaperone Hsp70 activates protein phosphatase 5 (PP5) by binding the tetratricopeptide repeat (TPR) domain.The Journal of biological chemistry · 2014Article
- SGTA: a new player in the molecular co-chaperone game.Hormones & cancer · 2013Review
- Up-regulation of SGTB is associated with neuronal apoptosis after neuroinflammation induced by lipopolysaccharide.Journal of molecular histology · 2013Article
- The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.Biochemistry · 2013Article
- Metaproteome analysis of endodontic infections in association with different clinical conditions.PloS one · 2013Article
- Hsp70 protein complexes as drug targets.Current pharmaceutical design · 2013Review
- Chaperone receptors: guiding proteins to intracellular compartments.Protoplasma · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A group of tetratricopeptide repeat (TPR)-containing proteins has been shown to interact with the C-terminal domain of the 70 kDa heat-shock cognate protein (hsc70). In the present study, the effect of the TPR-containing proteins, including the C-terminus of hsc70-interacting protein (CHIP), TPR1 and human glutamine-rich TPR-containing protein (hSGT), on refolding of luciferase by DnaJ and hsc70 was investigated. These proteins inhibited the restoration of luciferase activity by the chaperones. The inhibitory effect exerted by TPR1 and hSGT depended upon their binding to hsc70. However, the interaction with hsc70 did not appear to be required for the inhibition of luciferase refolding by CHIP. We also demonstrate that the peptide, GPTIEEVD, corresponding to the C-terminal end of hsc70, abolished the association of [(3)H]hsc70 with CHIP, TPR1 and hSGT. This implied that the GPTIEEVD motif of hsc70 was responsible for interacting with these TPR-containing proteins. However, the GGXP-repeats (where X is any aliphatic residue), another C-terminal conserved motif of vertebrate hsc70s, were not essential for interacting with the TPR-containing proteins. On the basis of mutagenesis studies, it was clear that a unique combination of the functional groups in the GPTIEEVD motif were utilized to interact with each TPR-containing protein, suggesting that inhibitors can be designed and used to elucidate the functional role of these interactions.
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