2014
DOI: 10.2174/1389203715666140331110522
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System Level Mechanisms of Adaptation, Learning, Memory Formation and Evolvability: The Role of Chaperone and Other Networks

Abstract: During the last decade, network approaches became a powerful tool to describe protein structure and dynamics. Here, we describe first the protein structure networks of molecular chaperones, then characterize chaperone containing sub-networks of interactomes called as chaperone-networks or chaperomes. We review the role of molecular chaperones in short-term adaptation of cellular networks in response to stress, and in long-term adaptation discussing their putative functions in the regulation of evolvability. We… Show more

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Cited by 10 publications
(9 citation statements)
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References 175 publications
(241 reference statements)
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“…Sharing functions of up-regulated genes -binding, transporter and catalytic activities -were complemented by signal transducer activity in BA10L and by receptor activity in BA10R ( Figure 1A). GO analysis of protein classes demonstrated strong increase in diversity of protein classes up-regulated in BA10R compared to BA10L, extending the latter with calcium binding proteins, cell adhesion molecules, receptors, chaperones, extracellular matrix proteins and other classes known to be involved in neuronal plasticity (Baucum, 2017;Dzyubenko, Gottschling, & Faissner, 2016;Gyurko, Soti, Stetak, & Csermely, 2014;Sheng, Leshchyns'ka, & Sytnyk 2013) ( Figure 1B).…”
Section: Resultsmentioning
confidence: 97%
“…Sharing functions of up-regulated genes -binding, transporter and catalytic activities -were complemented by signal transducer activity in BA10L and by receptor activity in BA10R ( Figure 1A). GO analysis of protein classes demonstrated strong increase in diversity of protein classes up-regulated in BA10R compared to BA10L, extending the latter with calcium binding proteins, cell adhesion molecules, receptors, chaperones, extracellular matrix proteins and other classes known to be involved in neuronal plasticity (Baucum, 2017;Dzyubenko, Gottschling, & Faissner, 2016;Gyurko, Soti, Stetak, & Csermely, 2014;Sheng, Leshchyns'ka, & Sytnyk 2013) ( Figure 1B).…”
Section: Resultsmentioning
confidence: 97%
“…The pharmacological inhibition of HSP 90 has been associated with neurodegenerative disease, suggesting the protective role of these proteins (Luo et al, 2010). Recent evidence has suggested their role in the enhancement of memory formation (Gyurko et al, 2014). Another chaperone protein that is important in the quality control of protein folding is disulfide-isomerase A3, which is an enzyme in the endoplasmic reticulum of eukaryotic cells that acts as a binding partner for other proteins and has a role in myelin sheath preservation.…”
Section: Discussionmentioning
confidence: 99%
“…Included in this family are HSC70 (heat shock cognate, the constitutive form), HSP70 (the inducible form, also referred to as HSP72) and GRP-75 (a constitutively expressed glucose-regulated protein found in the endoplasmic reticulum) [ 5 ]. Heat shock proteins 70 function in co- and post-translational folding and the quality control of misfolded proteins [ 38 ]. More specifically, HSP70 participate in folding and assembly of newly synthesized proteins into macromolecular complexes; aggregation prevention; dissolution and refolding of aggregated proteins; as well as protein degradation [ 20 ].…”
Section: Cellular Stress Response and The Vitagene Systemmentioning
confidence: 99%
“…However, chaperone-based inhibitors do not interact with the effector proteins, but inhibit the ability of the associated chaperone(s) to maintain their activation-competent conformation. As a result, the client proteins became degraded by the proteasome [ 38 ]. Due to its biological relevance in the folding, maturation and stabilization of pro-tumorigenic client proteins, HSP90 is emerging as therapeutic target in cancer treatment, representing a viable drug target for the design of chemotherapies [ 38 ].…”
Section: Cellular Stress Response and The Vitagene Systemmentioning
confidence: 99%