The PDB and protein homeostasis: From chaperones to degradation and disaggregase machines

Saibil, Helen R.

doi:10.1016/j.jbc.2021.100744

Cited by 10 publications

(7 citation statements)

References 34 publications

(16 reference statements)

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“…In the liver, there is good evidence for circadian regulation of autophagy (109), and in fibroblasts, rhythms of proteasomal activity have been observed (110). In addition, a number of molecular chaperones, including heat shock proteins (Hsp70, Hsp90), are pivotal in protein folding and unfolding (111). The DNA binding of heat shock factor 1 (HSF1) is highly rhythmic (112) and drives the expression of heat shock proteins at the onset of activity.…”

Section: Proteostasismentioning

confidence: 99%

Defining circadian disruption in neurodegenerative disorders

Colwell¹

2021

Journal of Clinical Investigation

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Section: Proteostasismentioning

confidence: 99%

Defining circadian disruption in neurodegenerative disorders

Colwell¹

2021

Journal of Clinical Investigation

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“…For HSP70, two conformational states have been described, denoted as open and closed [ 74 , 80 ], or domain-docked and domain-undocked, respectively [ 113 ] ( Figure 1 a,b). In the closed state, ADP is bound in the nucleotide pocket of the HSP70 NBD and the SBD forms a closed cavity, binding client substrates with high affinity.…”

Section: The 70-kda Heat Shock Proteins (Hsp70s)mentioning

confidence: 99%

“…The structural rearrangements trigger the clamping down/closure of the SBDα onto an unfolded protein, preventing its dissociation and allowing its folding. The replacement of ADP with ATP gives rise to further conformational changes leading to the open state, when the flexible linker becomes ordered, and the α-helical lid of the SBD is held open by an interaction with the ATPase region of the NBD [ 80 , 113 ].…”

Section: The 70-kda Heat Shock Proteins (Hsp70s)mentioning

confidence: 99%

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Mitochondrial HSP70 Chaperone System—The Influence of Post-Translational Modifications and Involvement in Human Diseases

Havalová¹,

Ondrovičová²,

Keresztesová³

et al. 2021

IJMS

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Since their discovery, heat shock proteins (HSPs) have been identified in all domains of life, which demonstrates their importance and conserved functional role in maintaining protein homeostasis. Mitochondria possess several members of the major HSP sub-families that perform essential tasks for keeping the organelle in a fully functional and healthy state. In humans, the mitochondrial HSP70 chaperone system comprises a central molecular chaperone, mtHSP70 or mortalin (HSPA9), which is actively involved in stabilizing and importing nuclear gene products and in refolding mitochondrial precursor proteins, and three co-chaperones (HSP70-escort protein 1—HEP1, tumorous imaginal disc protein 1—TID-1, and Gro-P like protein E—GRPE), which regulate and accelerate its protein folding functions. In this review, we summarize the roles of mitochondrial molecular chaperones with particular focus on the human mtHsp70 and its co-chaperones, whose deregulated expression, mutations, and post-translational modifications are often considered to be the main cause of neurological disorders, genetic diseases, and malignant growth.

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“…Today, many millions of PDB data consumers worldwide working in fundamental biology, biomedicine, bioengineering, biotechnology, and energy sciences enjoy no-cost access to 3D biostructure information with no limitations on data usage. Many scientific research areas have been profoundly impacted by the creation and availability of the PDB archive [ 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 , 39 , 40 , 41 , 42 ].…”

Section: Introductionmentioning

confidence: 99%

Protein Data Bank: A Comprehensive Review of 3D Structure Holdings and Worldwide Utilization by Researchers, Educators, and Students

et al. 2022

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The Research Collaboratory for Structural Bioinformatics Protein Data Bank (RCSB PDB), funded by the United States National Science Foundation, National Institutes of Health, and Department of Energy, supports structural biologists and Protein Data Bank (PDB) data users around the world. The RCSB PDB, a founding member of the Worldwide Protein Data Bank (wwPDB) partnership, serves as the US data center for the global PDB archive housing experimentally-determined three-dimensional (3D) structure data for biological macromolecules. As the wwPDB-designated Archive Keeper, RCSB PDB is also responsible for the security of PDB data and weekly update of the archive. RCSB PDB serves tens of thousands of data depositors (using macromolecular crystallography, nuclear magnetic resonance spectroscopy, electron microscopy, and micro-electron diffraction) annually working on all permanently inhabited continents. RCSB PDB makes PDB data available from its research-focused RCSB.org web portal at no charge and without usage restrictions to many millions of PDB data consumers around the globe. It also provides educators, students, and the general public with an introduction to the PDB and related training materials through its outreach and education-focused web portal, PDB101.RCSB.org. This review article describes growth of the PDB, examines evolution of experimental methods for structure determination viewed through the lens of the PDB archive, and provides a detailed accounting of PDB archival holdings and their utilization by researchers, educators, and students worldwide.

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The PDB and protein homeostasis: From chaperones to degradation and disaggregase machines

Cited by 10 publications

References 34 publications

Defining circadian disruption in neurodegenerative disorders

Defining circadian disruption in neurodegenerative disorders

Mitochondrial HSP70 Chaperone System—The Influence of Post-Translational Modifications and Involvement in Human Diseases

Protein Data Bank: A Comprehensive Review of 3D Structure Holdings and Worldwide Utilization by Researchers, Educators, and Students

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