scholarly journals Tumorous imaginal disc 1 (TID1) inhibits isoproterenol-induced cardiac hypertrophy and apoptosis by regulating c-terminus of hsc70-interacting protein (CHIP) mediated degradation of Gαs

2018 ◽  
Vol 15 (13) ◽  
pp. 1537-1546 ◽  
Author(s):  
Chih-Chung Feng ◽  
Po-Hsiang Liao ◽  
Hsiang-I Tsai ◽  
Shiu-Min Cheng ◽  
Liang-Yo Yang ◽  
...  
Keyword(s):  
Cardiac Hypertrophy ◽  
Imaginal Disc ◽  
Protein Chip ◽  
Interacting Protein ◽  
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.

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

scholarly journals USP47 and C Terminus of Hsp70-Interacting Protein (CHIP) Antagonistically Regulate Katanin-p60-Mediated Axonal Growth

2013 ◽  
Vol 33 (31) ◽  
pp. 12728-12738 ◽  
Author(s):  
S. W. Yang ◽  
K. H. Oh ◽  
E. Park ◽  
H. M. Chang ◽  
J. M. Park ◽  
...  
Keyword(s):  
Axonal Growth ◽  
Protein Chip ◽  
Interacting Protein ◽  
C Terminus
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