scholarly journals Protein quality control at the inner nuclear membrane

Nature ◽  
2014 ◽  
Vol 516 (7531) ◽  
pp. 410-413 ◽  
Author(s):  
Anton Khmelinskii ◽  
Ewa Blaszczak ◽  
Marina Pantazopoulou ◽  
Bernd Fischer ◽  
Deike J. Omnus ◽  
...  
Keyword(s):  
Quality Control ◽  
Nuclear Membrane ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Inner Nuclear Membrane

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
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