scholarly journals In the Heat of the Moment: ZTL-Mediated Protein Quality Control at High Temperatures

2017 ◽  
Vol 29 (11) ◽  
pp. 2685-2686
Author(s):  
Patrice A. Salomé
Keyword(s):  
Quality Control ◽  
High Temperatures ◽  
Protein Quality ◽  
Protein Quality Control ◽  
The Moment

Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates

2021 ◽  
pp. 153537022199981
Author(s):  
Chamithi Karunanayake ◽  
Richard C Page
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Structural Features ◽  
Cellular Protein ◽  
Mechanisms Of Action ◽  
Control Mechanisms ◽  
Nucleotide Exchange ◽  
Domain Organization ◽  
Nucleotide Exchange Factors

The chaperone heat shock protein 70 (Hsp70) and its network of co-chaperones serve as a central hub of cellular protein quality control mechanisms. Domain organization in Hsp70 dictates ATPase activity, ATP dependent allosteric regulation, client/substrate binding and release, and interactions with co-chaperones. The protein quality control activities of Hsp70 are classified as foldase, holdase, and disaggregase activities. Co-chaperones directly assisting protein refolding included J domain proteins and nucleotide exchange factors. However, co-chaperones can also be grouped and explored based on which domain of Hsp70 they interact. Here we discuss how the network of cytosolic co-chaperones for Hsp70 contributes to the functions of Hsp70 while closely looking at their structural features. Comparison of domain organization and the structures of co-chaperones enables greater understanding of the interactions, mechanisms of action, and roles played in protein quality control.

scholarly journals The protein quality control and neurodegeneration

2003 ◽  
Vol 122 (1) ◽  
pp. 30-36 ◽  
Author(s):  
Keiji TANAKA ◽  
Shigeo MURATA
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Protein Quality Control

scholarly journals TTC3-Mediated Protein Quality Control, A Potential Mechanism for Cognitive Impairment

2021 ◽  
Author(s):  
Xu Zhou ◽  
Xiongjin Chen ◽  
Tingting Hong ◽  
Miaoping Zhang ◽  
Yujie Cai ◽  
...  
Keyword(s):  
Quality Control ◽  
Cognitive Impairment ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Ubiquitin Proteasome System ◽  
Research Progress ◽  
Repeat Domain ◽  
Ubiquitin Proteasome ◽  
Domain 3

AbstractThe tetrapeptide repeat domain 3 (TTC3) gene falls within Down's syndrome (DS) critical region. Cognitive impairment is a common phenotype of DS and Alzheimer’s disease (AD), and overexpression of TTC3 can accelerate cognitive decline, but the specific mechanism is unknown. The TTC3-mediated protein quality control (PQC) mechanism, similar to the PQC system, is divided into three parts: it acts as a cochaperone to assist proteins in folding correctly; it acts as an E3 ubiquitin ligase (E3s) involved in protein degradation processes through the ubiquitin–proteasome system (UPS); and it may also eventually cause autophagy by affecting mitochondrial function. Thus, this article reviews the research progress on the structure, function, and metabolism of TTC3, including the recent research progress on TTC3 in DS and AD; the role of TTC3 in cognitive impairment through PQC in combination with the abovementioned attributes of TTC3; and the potential targets of TTC3 in the treatment of such diseases.

scholarly journals Autophagy and p62 in cardiac protein quality control

Autophagy ◽  
2011 ◽  
Vol 7 (11) ◽  
pp. 1382-1383 ◽  
Author(s):  
Huabo Su ◽  
Xuejun Wang
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Protein Quality Control

scholarly journals NEMF mutations that impair ribosome-associated quality control are associated with neuromuscular disease

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Paige B. Martin ◽  
Yu Kigoshi-Tansho ◽  
Roger B. Sher ◽  
Gianina Ravenscroft ◽  
Jennifer E. Stauffer ◽  
...  
Keyword(s):  
Quality Control ◽  
Nervous System ◽  
Mouse Models ◽  
Human Disease ◽  
Neuromuscular Disease ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Motor Neuron Degeneration ◽  
Neuron Degeneration ◽  
Ribosome Stalling

Abstract A hallmark of neurodegeneration is defective protein quality control. The E3 ligase Listerin (LTN1/Ltn1) acts in a specialized protein quality control pathway—Ribosome-associated Quality Control (RQC)—by mediating proteolytic targeting of incomplete polypeptides produced by ribosome stalling, and Ltn1 mutation leads to neurodegeneration in mice. Whether neurodegeneration results from defective RQC and whether defective RQC contributes to human disease have remained unknown. Here we show that three independently-generated mouse models with mutations in a different component of the RQC complex, NEMF/Rqc2, develop progressive motor neuron degeneration. Equivalent mutations in yeast Rqc2 selectively interfere with its ability to modify aberrant translation products with C-terminal tails which assist with RQC-mediated protein degradation, suggesting a pathomechanism. Finally, we identify NEMF mutations expected to interfere with function in patients from seven families presenting juvenile neuromuscular disease. These uncover NEMF’s role in translational homeostasis in the nervous system and implicate RQC dysfunction in causing neurodegeneration.

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