The Proteostasis Network's Various Roles for Small Heat Shock Proteins
This special issue belongs to
|International Journal of Molecular Biotechnology
Deadline for Manuscript Submission
|March 31st, 2022
Deadline for Publication
|April 15, 2022
Special Issue Description
By preventing the buildup of misfolded protein conformers, the protein quality control (PQC) system preserves protein homeostasis. Major tactics used by ATP-dependent proteases and chaperones to degrade and refold substrates make up the proteostasis network. The ATP-independent chaperones known as small heat shock proteins bind to misfolded proteins to stop their uncontrolled aggregation. The conserved-crystallin domain (ACD) is shared by all sHsps, but their N- and C-terminal extensions are varied and generally disordered, giving them functional specialization (NTE, CTE).
They are created by numerous, weak contacts between NTE/CTEs and ACD dimers and take the shape of huge, polydisperse oligomers. Due to the enormous heterogeneity of sHsp oligomers and the sequence changes of sHsps, sHsps can perform a variety of functions in the PQC network. When under stress, sHsp oligomers represent dynamic, inactive resting states that are quickly oligomerized and activated, releasing substrate binding sites in NTEs and ACDs. Large sHsp/substrate complexes are typically used to isolate bound substrates. The proteostasis network's third strategy is represented by the sequestration activity of sHsps. The burden on other PQC components under conditions of acute and ongoing stress is lessened by substrate sequestration. ATP-dependent Hsp70/Hsp100 chaperones can release sequestered substrates and drive them toward refolding pathways, or they can sort them for degradation by autophagic pathways.
* Autophagic pathways
* Polydisperse oligomers
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