Carboxyl terminus of heat-shock cognate 70-interacting protein degrades tau regardless its phosphorylation status without affecting the spatial memory of the rats

2008 ◽  
Vol 115 (3) ◽  
pp. 483-491 ◽  
Author(s):  
Y.-J. Zhang ◽  
Y.-F. Xu ◽  
X.-H. Liu ◽  
D. Li ◽  
J. Yin ◽  
...  
Keyword(s):  
Heat Shock ◽  
Spatial Memory ◽  
Carboxyl Terminus ◽  
Interacting Protein ◽  
Heat Shock Cognate 70

scholarly journals C-Terminus of Heat Shock Cognate 70 Interacting Protein Increases Following Stroke and Impairs Survival Against Acute Oxidative Stress

2011 ◽  
Vol 14 (10) ◽  
pp. 1787-1801 ◽  
Author(s):  
Jeannette N. Stankowski ◽  
Stephanie L.H. Zeiger ◽  
Evan L. Cohen ◽  
Donald B. DeFranco ◽  
Jiyang Cai ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Interacting Protein ◽  
C Terminus ◽  
Heat Shock Cognate 70

scholarly journals MKKS Is a Centrosome-shuttling Protein Degraded by Disease-causing Mutations via CHIP-mediated Ubiquitination

2008 ◽  
Vol 19 (3) ◽  
pp. 899-911 ◽  
Author(s):  
Shoshiro Hirayama ◽  
Yuji Yamazaki ◽  
Akira Kitamura ◽  
Yukako Oda ◽  
Daisuke Morito ◽  
...  
Keyword(s):  
Heat Shock ◽  
Ubiquitin Ligase ◽  
Wild Type ◽  
Hsp 70 ◽  
Human Genetic Disease ◽  
Interacting Protein ◽  
Bardet Biedl Syndrome ◽  
Heat Shock Cognate 70 ◽  
Ubiquitin Proteasome ◽  
Proteasome Pathway

McKusick–Kaufman syndrome (MKKS) is a recessively inherited human genetic disease characterized by several developmental anomalies. Mutations in the MKKS gene also cause Bardet–Biedl syndrome (BBS), a genetically heterogeneous disorder with pleiotropic symptoms. However, little is known about how MKKS mutations lead to disease. Here, we show that disease-causing mutants of MKKS are rapidly degraded via the ubiquitin–proteasome pathway in a manner dependent on HSC70 interacting protein (CHIP), a chaperone-dependent ubiquitin ligase. Although wild-type MKKS quickly shuttles between the centrosome and cytosol in living cells, the rapidly degraded mutants often fail to localize to the centrosome. Inhibition of proteasome functions causes MKKS mutants to form insoluble structures at the centrosome. CHIP and partner chaperones, including heat-shock protein (HSP)70/heat-shock cognate 70 and HSP90, strongly recognize MKKS mutants. Modest knockdown of CHIP by RNA interference moderately inhibited the degradation of MKKS mutants. These results indicate that the MKKS mutants have an abnormal conformation and that chaperone-dependent degradation mediated by CHIP is a key feature of MKKS/BBS diseases.

scholarly journals Dodecin as carrier protein for immunizations and bioengineering applications

2020 ◽  
Author(s):  
Florian Bourdeaux ◽  
Yannick Kopp ◽  
Julia Lautenschläger ◽  
Ines Gößner ◽  
Hüseyin Besir ◽  
...  
Keyword(s):  
Heat Shock ◽  
Fluorescent Protein ◽  
Spherical Shape ◽  
Interacting Protein ◽  
C Terminus ◽  
Heat Shock Cognate 70 ◽  
A Cell ◽  
Green Fluorescent ◽  
Shock Proteins

AbstractIn bioengineering, scaffold proteins have been increasingly used to recruit molecules to parts of a cell, or to enhance the efficacy of biosynthetic or signaling pathways. For example, scaffolds can be used to make weak or non-immunogenic small molecules immunogenic by attaching them to the scaffold, in this role called carrier. Here, we present the dodecin from Mycobacterium tuberculosis (mtDod) as a new scaffold protein. MtDod is a homododecameric complex of spherical shape, high stability and robust assembly, which allows the attachment of cargo at its surface. We show that mtDod, either directly loaded with cargo or equipped with domains for non-covalent and covalent loading of cargo, can be produced recombinantly in high quantity and quality in Escherichia coli. Fusions of mtDod with proteins of up to four times the size of mtDod, e.g. with monomeric superfolder green fluorescent protein creating a 437 kDa large dodecamer, were successfully purified, showing mtDod’s ability to function as recruitment hub. Further, mtDod equipped with SYNZIP and SpyCatcher domains for post-translational recruitment of cargo was prepared of which the mtDod/SpyCatcher system proved to be particularly useful. In a case study, we finally show that mtDod peptide fusions allow producing antibodies against human heat shock proteins and the C-terminus of heat shock cognate 70 interacting protein (CHIP).For Table of Contents Only

Carboxyl Terminus of Heat Shock Protein 70-Interacting Protein Inhibits Angiotensin II-Induced Cardiac Remodeling

2012 ◽  
Vol 25 (9) ◽  
pp. 994-1001 ◽  
Author(s):  
Kun Yang ◽  
Tian-Peng Zhang ◽  
Cui Tian ◽  
Li-xin Jia ◽  
Jie Du ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cardiac Remodeling ◽  
Heat Shock Protein 70 ◽  
Carboxyl Terminus ◽  
Interacting Protein
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