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Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes
Heat shock proteins (HSP) are critical elements for the preservation of cellular homeostasis by participating in an array of biological processes. In addition, HSP play an important role in cellular protection from various environmental stresses. HSP are part of a large family of different molecular...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Netherlands
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8129608/ https://www.ncbi.nlm.nih.gov/pubmed/34003451 http://dx.doi.org/10.1007/s12192-021-01210-8 |
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author | Dores-Silva, Paulo R. Cauvi, David M. Coto, Amanda L. S. Silva, Noeli S. M. Borges, Júlio C. De Maio, Antonio |
author_facet | Dores-Silva, Paulo R. Cauvi, David M. Coto, Amanda L. S. Silva, Noeli S. M. Borges, Júlio C. De Maio, Antonio |
author_sort | Dores-Silva, Paulo R. |
collection | PubMed |
description | Heat shock proteins (HSP) are critical elements for the preservation of cellular homeostasis by participating in an array of biological processes. In addition, HSP play an important role in cellular protection from various environmental stresses. HSP are part of a large family of different molecular mass polypeptides, displaying various expression patterns, subcellular localizations, and diversity functions. An unexpected observation was the detection of HSP on the cell surface. Subsequent studies have demonstrated that HSP have the ability to interact and penetrate lipid bilayers by a process initiated by the recognition of phospholipid heads, followed by conformational changes, membrane insertion, and oligomerization. In the present study, we described the interaction of HSPA8 (HSC70), the constitutive cytosolic member of the HSP70 family, with lipid membranes. HSPA8 showed high selectivity for negatively charged phospholipids, such as phosphatidylserine and cardiolipin, and low affinity for phosphatidylcholine. Membrane insertion was mediated by a spontaneous process driven by increases in entropy and diminished by the presence of ADP or ATP. Finally, HSPA8 was capable of driving into the lipid bilayer HSP90 that does not display any lipid biding capacity by itself. This observation suggests that HSPA8 may act as a membrane chaperone. |
format | Online Article Text |
id | pubmed-8129608 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Springer Netherlands |
record_format | MEDLINE/PubMed |
spelling | pubmed-81296082021-05-18 Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes Dores-Silva, Paulo R. Cauvi, David M. Coto, Amanda L. S. Silva, Noeli S. M. Borges, Júlio C. De Maio, Antonio Cell Stress Chaperones Original Paper Heat shock proteins (HSP) are critical elements for the preservation of cellular homeostasis by participating in an array of biological processes. In addition, HSP play an important role in cellular protection from various environmental stresses. HSP are part of a large family of different molecular mass polypeptides, displaying various expression patterns, subcellular localizations, and diversity functions. An unexpected observation was the detection of HSP on the cell surface. Subsequent studies have demonstrated that HSP have the ability to interact and penetrate lipid bilayers by a process initiated by the recognition of phospholipid heads, followed by conformational changes, membrane insertion, and oligomerization. In the present study, we described the interaction of HSPA8 (HSC70), the constitutive cytosolic member of the HSP70 family, with lipid membranes. HSPA8 showed high selectivity for negatively charged phospholipids, such as phosphatidylserine and cardiolipin, and low affinity for phosphatidylcholine. Membrane insertion was mediated by a spontaneous process driven by increases in entropy and diminished by the presence of ADP or ATP. Finally, HSPA8 was capable of driving into the lipid bilayer HSP90 that does not display any lipid biding capacity by itself. This observation suggests that HSPA8 may act as a membrane chaperone. Springer Netherlands 2021-05-18 2021-07 /pmc/articles/PMC8129608/ /pubmed/34003451 http://dx.doi.org/10.1007/s12192-021-01210-8 Text en © Cell Stress Society International 2021 |
spellingShingle | Original Paper Dores-Silva, Paulo R. Cauvi, David M. Coto, Amanda L. S. Silva, Noeli S. M. Borges, Júlio C. De Maio, Antonio Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes |
title | Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes |
title_full | Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes |
title_fullStr | Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes |
title_full_unstemmed | Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes |
title_short | Human heat shock cognate protein (HSC70/HSPA8) interacts with negatively charged phospholipids by a different mechanism than other HSP70s and brings HSP90 into membranes |
title_sort | human heat shock cognate protein (hsc70/hspa8) interacts with negatively charged phospholipids by a different mechanism than other hsp70s and brings hsp90 into membranes |
topic | Original Paper |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8129608/ https://www.ncbi.nlm.nih.gov/pubmed/34003451 http://dx.doi.org/10.1007/s12192-021-01210-8 |
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