scholarly journals Protein Quality Control in Health and Disease

2016 ◽  
Vol 9 (3) ◽  
pp. a023523 ◽  
Author(s):  
Tatyana Dubnikov ◽  
Tziona Ben-Gedalya ◽  
Ehud Cohen
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Health And Disease

scholarly journals Neddylation, an Emerging Mechanism Regulating Cardiac Development and Function

2020 ◽  
Vol 11 ◽  
Author(s):  
Jie Li ◽  
Jianqiu Zou ◽  
Rodney Littlejohn ◽  
Jinbao Liu ◽  
Huabo Su
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Cardiac Development ◽  
Current Knowledge ◽  
Biological Significance ◽  
Protein Quality Control ◽  
Pathogenic Factors ◽  
Health And Disease ◽  
The Stability ◽  
And Function

Defects in protein quality control have been increasingly recognized as pathogenic factors in the development of heart failure, a persistent devastating disease lacking efficacious therapies. Ubiquitin and ubiquitin-like proteins, a family of post-translational modifying polypeptides, play important roles in controlling protein quality by maintaining the stability and functional diversity of the proteome. NEDD8 (neural precursor cell expressed, developmentally downregulated 8), a small ubiquitin-like protein, was discovered two decades ago but until recently the biological significance of NEDD8 modifications (neddylation) in the heart has not been appreciated. In this review, we summarize the current knowledge of the biology of neddylation, highlighting several mechanisms by which neddylation regulates the function of its downstream targets, and discuss the expanding roles for neddylation in cardiac physiology and disease, with an emphasis on cardiac protein quality control. Finally, we outline challenges linked to the study of neddylation in health and disease.

The Giant Protein Titin as an Integrator of Myocyte Signaling Pathways

Physiology ◽  
2010 ◽  
Vol 25 (3) ◽  
pp. 186-198 ◽  
Author(s):  
Wolfgang A. Linke ◽  
Martina Krüger
Keyword(s):  
Quality Control ◽  
Signaling Pathways ◽  
Protein Interactions ◽  
Protein Quality ◽  
Muscle Protein ◽  
Gene Activation ◽  
Protein Quality Control ◽  
Control Mechanisms ◽  
Protein Protein Interactions ◽  
Health And Disease

The giant muscle protein titin, the “backbone” of the sarcomere, harbors a complex molecular spring whose stiffness is variably tuned in health and disease. Titin is increasingly recognized as a crucial integrator of diverse myocyte signaling pathways. The titin-associated signalosome includes hotspots of protein-protein interactions important for the regulation of protein quality-control mechanisms, hypertrophic gene activation, and mechanosensing.

scholarly journals Mitochondrial protein quality control in health and disease

2014 ◽  
Vol 171 (8) ◽  
pp. 1870-1889 ◽  
Author(s):  
Michael J Baker ◽  
Catherine S Palmer ◽  
Diana Stojanovski
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Mitochondrial Protein ◽  
Protein Quality Control ◽  
Health And Disease

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.

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