CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

By L. Petrucelli, Dennis W. Dickson, K. Kehoe, Julie P. Taylor, H. Snyder, A. Grover, M. D. Lucia, E. McGowan, Jada Lewis, G. Prihar and 10 more. 2004

740 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Physiology

View Paper: https://www.semanticscholar.org/paper/5ba4f4d55ed7deb7e1c520538e840246340ad3c7

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Cell Biology

1. Susmita Kaushik
2. D. Rubinsztein
3. Esther Wong
4. A. Cuervo
5. Cahir O'Kane
6. M. Eddins
7. E. Mandelkow
8. L. Mucke

In Molecular Biology

1. Fei Liu
2. C. Gong
3. K. Iqbal
4. I. Grundke‐Iqbal
5. Fiona M Menzies
6. M. Eddins
7. Tapan H. Mehta
8. A. Cuervo

In Physiology

1. Fei Liu
2. C. Gong
3. K. Iqbal
4. I. Grundke‐Iqbal
5. A. Cuervo
6. D. Rubinsztein
7. Dennis W. Dickson
8. L. Mucke

Citations in the corpus

• Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020, background): “Induction of Hsp70 by geldanamycin promotes tau degradation both in vitro and in vivo, whereas deletion of CHIP increases the accumulation of phosphorylated tau and caspase-3 cleaved tau [167, 171].”
• The Many Faces of Tau (2011, background): “Some tau aggregation inhibitors are effective in Neuro2A cell lines overexpressing a 4R tau microtubule repeat domain fragment with a K280 deletion, which promotes its aggregation (Pickhardt et al., 2005).”
• Acetylation of tau inhibits its degradation and contributes to tauopathy. (2010, neutral): “The E3 ubiquitin ligase CHIP (carboxyl terminus of the Hsc70-interacting protein) is involved in polyubiquitination and degradation of p-tau (Petrucelli et al., 2004; Shimura et al., 2004).”
• Ubiquitin: structures, functions, mechanisms. (2004, background): “CHIP substrates that conform to this paradigm include the cystic fibrosis transmembrane receptor [112], the glucocorticoid receptor [113], and tau [114,115].”
• Rapamycin alleviates toxicity of different aggregate-prone proteins. (2006, methodology): “We then analysed the effects of rapamycin treatment on the most common tau mutation, P301L, that has been extensively studied both in cells and in mouse transgenics (33,34) and that exhibits strong aggregation properties (35).”
• Mechanisms of tau-induced neurodegeneration (2009, positive): “Overexpression of Hsp70, which interacts with the heatshock cognate (Hsc) 70-interacting protein (CHIP), a ubiquitin ligase, causes a reduction of tau in transgenic mice [154].”
• Biochemistry and cell biology of tau protein in neurofibrillary degeneration. (2012, background): “It participates in the protein triage process whereby the chaperone system decides whether to keep the protein for refolding or to send it to the proteasome for degradation (Petrucelli et al. 2004; Shimura et al. 2004b).”
• Tar DNA Binding Protein-43 (TDP-43) Associates with Stress Granules: Analysis of Cultured Cells and Pathological Brain Tissue (2010, background): “Reversible aggregation has been noted in other systems, such as the interaction of tau with CHIP [45,46].”
• Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing. (2009, background): “In AD brain, hsc70 is associated with neurofibrillary tangles (36) and has been described to interact with Tau (19).”
• The high-affinity HSP90-CHIP complex recognizes and selectively degrades phosphorylated tau client proteins. (2007, methodology): “Molecular chaperones are capable of reducing p-tau concentrations and have been shown to prevent tau-associated cellular toxicity (10, 11).”