Service quality control mechanisms in franchise networks

2011 ◽  
Vol 31 (5) ◽  
pp. 713-723 ◽  
Author(s):  
Roberto Sánchez Gómez ◽  
Isabel Suárez González ◽  
Luis Vazquez Suárez
Keyword(s):  
Quality Control ◽  
Service Quality ◽  
Control Mechanisms ◽  
Franchise Networks

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 COVID-19 Brings Data Equity Challenges to the Fore

2021 ◽  
Author(s):  
H.V. Jagadish ◽  
Julia Stoyanovich ◽  
Bill Howe
Keyword(s):  
Quality Control ◽  
Government Policy ◽  
Data Driven ◽  
Contact Tracing ◽  
Control Mechanisms ◽  
Sources Of Information ◽  
Decision Systems ◽  
Physical Resources ◽  
Multiple Levels ◽  
Data Driven Decisions

The COVID-19 pandemic is compelling us to make crucial data-driven decisions quickly, bringing together diverse and unreliable sources of information without the usual quality control mechanisms we may employ. These decisions are consequential at multiple levels: they can inform local, state and national government policy, be used to schedule access to physical resources such as elevators and workspaces within an organization, and inform contact tracing and quarantine actions for individuals. In all these cases, significant inequities are likely to arise, and to be propagated and reinforced by data-driven decision systems. In this article, we propose a framework, called FIDES, for surfacing and reasoning about data equity in these systems.

scholarly journals Limited ER quality control for GPI-anchored proteins

2016 ◽  
Vol 213 (6) ◽  
pp. 693-704 ◽  
Author(s):  
Natalia Sikorska ◽  
Leticia Lemus ◽  
Auxiliadora Aguilera-Romero ◽  
Javier Manzano-Lopez ◽  
Howard Riezman ◽  
...  
Keyword(s):  
Quality Control ◽  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Misfolded Proteins ◽  
Control Mechanisms ◽  
Gpi Anchor ◽  
Er Quality Control ◽  
Entire Class ◽  
Er Export ◽  
Export Signal

Endoplasmic reticulum (ER) quality control mechanisms target terminally misfolded proteins for ER-associated degradation (ERAD). Misfolded glycophosphatidylinositol-anchored proteins (GPI-APs) are, however, generally poor ERAD substrates and are targeted mainly to the vacuole/lysosome for degradation, leading to predictions that a GPI anchor sterically obstructs ERAD. Here we analyzed the degradation of the misfolded GPI-AP Gas1* in yeast. We could efficiently route Gas1* to Hrd1-dependent ERAD and provide evidence that it contains a GPI anchor, ruling out that a GPI anchor obstructs ERAD. Instead, we show that the normally decreased susceptibility of Gas1* to ERAD is caused by canonical remodeling of its GPI anchor, which occurs in all GPI-APs and provides a protein-independent ER export signal. Thus, GPI anchor remodeling is independent of protein folding and leads to efficient ER export of even misfolded species. Our data imply that ER quality control is limited for the entire class of GPI-APs, many of them being clinically relevant.

scholarly journals Targeting Protein Quality Control Mechanisms by Natural Products to Promote Healthy Ageing

Molecules ◽  
2018 ◽  
Vol 23 (5) ◽  
pp. 1219 ◽  
Author(s):  
Sophia Wedel ◽  
Maria Manola ◽  
Maria Cavinato ◽  
Ioannis Trougakos ◽  
Pidder Jansen-Dürr
Keyword(s):  
Quality Control ◽  
Natural Products ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Healthy Ageing ◽  
Control Mechanisms

Capacity Design and Service Quality Control in a Queuing System

1977 ◽  
Vol 25 (4) ◽  
pp. 651-661 ◽  
Author(s):  
S. D. Deshmukh ◽  
Suresh Jain
Keyword(s):  
Quality Control ◽  
Service Quality ◽  
Queuing System ◽  
Capacity Design

scholarly journals Phosphorylation Modifications Regulating Cardiac Protein Quality Control Mechanisms

2020 ◽  
Vol 11 ◽  
Author(s):  
Sumita Mishra ◽  
Brittany L. Dunkerly-Eyring ◽  
Gizem Keceli ◽  
Mark J. Ranek
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Control Mechanisms

scholarly journals Spatial quality control bypasses cell-based limitations on proteostasis to promote prion curing

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Courtney L Klaips ◽  
Megan L Hochstrasser ◽  
Christine R Langlois ◽  
Tricia R Serio
Keyword(s):  
Quality Control ◽  
Molecular Chaperone ◽  
Protein Misfolding ◽  
Elevated Temperatures ◽  
Control Factor ◽  
Control Mechanisms ◽  
Cellular Environment ◽  
Effective Activity ◽  
Spatial Quality

The proteostasis network has evolved to support protein folding under normal conditions and to expand this capacity in response to proteotoxic stresses. Nevertheless, many pathogenic states are associated with protein misfolding, revealing in vivo limitations on quality control mechanisms. One contributor to these limitations is the physical characteristics of misfolded proteins, as exemplified by amyloids, which are largely resistant to clearance. However, other limitations imposed by the cellular environment are poorly understood. To identify cell-based restrictions on proteostasis capacity, we determined the mechanism by which thermal stress cures the [PSI+]/Sup35 prion. Remarkably, Sup35 amyloid is disassembled at elevated temperatures by the molecular chaperone Hsp104. This process requires Hsp104 engagement with heat-induced non-prion aggregates in late cell-cycle stage cells, which promotes its asymmetric retention and thereby effective activity. Thus, cell division imposes a potent limitation on proteostasis capacity that can be bypassed by the spatial engagement of a quality control factor.

Sign in / Sign up

Export Citation Format

Share Document