Corrigendum to “In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis”[Neurobiology of Disease 33/3 (2009) 342–353]

2012 ◽  
Vol 46 (2) ◽  
pp. 503
Author(s):  
Aislinn J. Williams ◽  
Tina M. Knutson ◽  
Veronica F. Colomer Gould ◽  
Henry L. Paulson
Keyword(s):  
Protein Chip ◽  
Interacting Protein ◽  
Aggregation Model ◽  
C Terminus

scholarly journals In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis

2009 ◽  
Vol 33 (3) ◽  
pp. 342-353 ◽  
Author(s):  
Aislinn J. Williams ◽  
Tina M. Knutson ◽  
Veronica F. Colomer Gould ◽  
Henry L. Paulson
Keyword(s):  
Protein Chip ◽  
Interacting Protein ◽  
Aggregation Model ◽  
C Terminus

scholarly journals The Chaperone-assisted E3 Ligase C Terminus of Hsc70-interacting Protein (CHIP) Targets PTEN for Proteasomal Degradation

2012 ◽  
Vol 287 (19) ◽  
pp. 15996-16006 ◽  
Author(s):  
Syed Feroj Ahmed ◽  
Satamita Deb ◽  
Indranil Paul ◽  
Anirban Chatterjee ◽  
Tapashi Mandal ◽  
...  
Keyword(s):  
E3 Ligase ◽  
Proteasomal Degradation ◽  
Protein Chip ◽  
Interacting Protein ◽  
C Terminus

scholarly journals Molecular Mechanism of the Negative Regulation of Smad1/5 Protein by Carboxyl Terminus of Hsc70-interacting Protein (CHIP)

2011 ◽  
Vol 286 (18) ◽  
pp. 15883-15894 ◽  
Author(s):  
Le Wang ◽  
Yi-Tong Liu ◽  
Rui Hao ◽  
Lei Chen ◽  
Zhijie Chang ◽  
...  
Keyword(s):  
Molecular Mechanism ◽  
Transforming Growth Factor ◽  
Transforming Growth Factor Β ◽  
Protein Chip ◽  
Independent Manner ◽  
Interacting Protein ◽  
Signaling Complex ◽  
Bone Morphogenetic Protein Pathway ◽  
C Terminus ◽  
Shock Proteins

The transforming growth factor-β (TGF-β) superfamily of ligands signals along two intracellular pathways, Smad2/3-mediated TGF-β/activin pathway and Smad1/5/8-mediated bone morphogenetic protein pathway. The C terminus of Hsc70-interacting protein (CHIP) serves as an E3 ubiquitin ligase to mediate the degradation of Smad proteins and many other signaling proteins. However, the molecular mechanism for CHIP-mediated down-regulation of TGF-β signaling remains unclear. Here we show that the extreme C-terminal sequence of Smad1 plays an indispensable role in its direct association with the tetratricopeptide repeat (TPR) domain of CHIP. Interestingly, Smad1 undergoes CHIP-mediated polyubiquitination in the absence of molecular chaperones, and phosphorylation of the C-terminal SXS motif of Smad1 enhances the interaction and ubiquitination. We also found that CHIP preferentially binds to Smad1/5 and specifically disrupts the core signaling complex of Smad1/5 and Smad4. We determined the crystal structures of CHIP-TPR in complex with the phosphorylated/pseudophosphorylated Smad1 peptides and with an Hsp70/Hsc70 C-terminal peptide. Structural analyses and subsequent biochemical studies revealed that the distinct CHIP binding affinities of Smad1/5 or Smad2/3 result from the nonconservative hydrophobic residues at R-Smad C termini. Unexpectedly, the C-terminal peptides from Smad1 and Hsp70/Hsc70 bind in the same groove of CHIP-TPR, and heat shock proteins compete with Smad1/5 for CHIP interaction and concomitantly suppress, rather than facilitate, CHIP-mediated Smad ubiquitination. Thus, we conclude that CHIP inhibits the signaling activities of Smad1/5 by recruiting Smad1/5 from the functional R-/Co-Smad complex and further promoting the ubiquitination/degradation of Smad1/5 in a chaperone-independent manner.

scholarly journals CHIP promotes Runx2 degradation and negatively regulates osteoblast differentiation

2008 ◽  
Vol 181 (6) ◽  
pp. 959-972 ◽  
Author(s):  
Xueni Li ◽  
Mei Huang ◽  
Huiling Zheng ◽  
Yinyin Wang ◽  
Fangli Ren ◽  
...  
Keyword(s):  
Transcriptional Activation ◽  
Osteoblast Differentiation ◽  
Degradation Mechanism ◽  
Interacting Protein ◽  
E3 Ligases ◽  
Protein Levels ◽  
C Terminus ◽  
Osteoblast Lineage

Runx2, an essential transactivator for osteoblast differentiation, is tightly regulated at both the transcriptional and posttranslational levels. In this paper, we report that CHIP (C terminus of Hsc70-interacting protein)/STUB1 regulates Runx2 protein stability via a ubiquitination-degradation mechanism. CHIP interacts with Runx2 in vitro and in vivo. In the presence of increased Runx2 protein levels, CHIP expression decreases, whereas the expression of other E3 ligases involved in Runx2 degradation, such as Smurf1 or WWP1, remains constant or increases during osteoblast differentiation. Depletion of CHIP results in the stabilization of Runx2, enhances Runx2-mediated transcriptional activation, and promotes osteoblast differentiation in primary calvarial cells. In contrast, CHIP overexpression in preosteoblasts causes Runx2 degradation, inhibits osteoblast differentiation, and instead enhances adipogenesis. Our data suggest that negative regulation of the Runx2 protein by CHIP is critical in the commitment of precursor cells to differentiate into the osteoblast lineage.

The Stability of Wild-type and Deletion Mutants of Human C-terminus Hsp70-interacting Protein (CHIP)

2013 ◽  
Vol 20 (5) ◽  
pp. 524-529 ◽  
Author(s):  
Isabel C.R. Millan ◽  
Ana L.A. Squillace ◽  
Lisandra M. Gava ◽  
Carlos H.I. Ramos
Keyword(s):  
Protein Chip ◽  
Deletion Mutants ◽  
Wild Type ◽  
Interacting Protein ◽  
C Terminus ◽  
The Stability
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