ArticleCell stress & chaperones2002
Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity.
Article in Cell stress & chaperones, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 59 citations in OpenAlex.
- Substrate relay in an Hsp70-cochaperone cascade safeguards tail-anchored membrane protein targeting.The EMBO journal · 2018Article
- SGTA-Dependent Regulation of Hsc70 Promotes Cytosol Entry of Simian Virus 40 from the Endoplasmic Reticulum.Journal of virology · 2017Article
- Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.Frontiers in molecular biosciences · 2017Article
- Review
- Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein Alpha (SGTA) Ablation Limits Offspring Viability and Growth in Mice.Scientific reports · 2016Article
- The Vpu-interacting Protein SGTA Regulates Expression of a Non-glycosylated Tetherin Species.Scientific reports · 2016Article
- Article
- Expression and prognostic role of SGTA in human breast carcinoma correlates with tumor cell proliferation.Journal of molecular histology · 2014Article
- A pipeline for determining protein-protein interactions and proximities in the cellular milieu.Molecular & cellular proteomics : MCP · 2014Article
- 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
- A cytosolic chaperone complexes with dynamic membrane J-proteins and mobilizes a nonenveloped virus out of the endoplasmic reticulum.PLoS pathogens · 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
- Expression and clinical role of small glutamine-rich tetratricopeptide repeat (TPR)-containing protein alpha (SGTA) as a novel cell cycle protein in NSCLC.Journal of cancer research and clinical oncology · 2013Article
- Clearance of yeast eRF-3 prion [PSI+] by amyloid enlargement due to the imbalance between chaperone Ssa1 and cochaperone Sgt2.Translation (Austin, Tex.) · 2013Article
- Regulation of chaperone effects on a yeast prion by cochaperone Sgt2.Molecular and cellular biology · 2012Article
- A structural model of the Sgt2 protein and its interactions with chaperones and the Get4/Get5 complex.The Journal of biological chemistry · 2011Article
- Versatile TPR domains accommodate different modes of target protein recognition and function.Cell stress & chaperones · 2011Review
- Overexpression of human virus surface glycoprotein precursors induces cytosolic unfolded protein response in Saccharomyces cerevisiae.Microbial cell factories · 2011Article
- Neuroproteomics: a biochemical means to discriminate the extent and modality of brain injury.Journal of neurotrauma · 2010Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Molecular chaperone complexes containing heat shock protein (Hsp) 70 and Hsp90 are regulated by cochaperones, including a subclass of regulators, such as Hsp70 interacting protein (Hip), C-terminus of Hsp70 interacting protein (CHIP), and Hsp70-Hsp90 organizing factor (Hop), that contain tetratricopeptide repeats (TPRs), where Hsp70 refers to Hsp70 and its nearly identical constitutive counterpart, Hsc70, together. These proteins interact with the Hsp70 to regulate adenosine triphosphatase (ATPase) and folding activities or to generate the chaperone complex. Here we provide evidence that small glutamine-rich protein/viral protein U-binding protein (SGT/UBP) is a cochaperone that negatively regulates Hsp70. By "Far-Western" and pull-down assays, SGT/UBP was shown to interact directly with Hsp70 and weakly with Hsp90. The interaction of SGT/UBP with both these protein chaperones was mapped to 3 TPRs in SGT/UBP (amino acids 95-195) that are flanked by charged residues. Moreover, SGT/UBP caused an approximately 30% reduction in both the intrinsic ATPase activity of Hsc70 and the ability of Hsc70 to refold denatured luciferase in vitro. This negative effect of SGT/UBP on Hsc70 is similar in magnitude to that observed for the cochaperone CHIP. A role for SGT/UBP in protein folding is also supported by evidence that a yeast strain containing a deletion in the yeast homolog to SGT/UBP (delta SGT/UBP) displays a 50-fold reduction in recovery from heat shock compared with the wild type parent. Together, these results are consistent with a regulatory role for SGT/UBP in the chaperone complex.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.