| Full text | |
| Author(s): |
Dores-Silva, Paulo R.
[1, 2]
;
Cauvi, David M.
[2]
;
Coto, Amanda L. S.
[1]
;
Silva, Noeli S. M.
[1]
;
Borges, Julio C.
[1]
;
De Maio, Antonio
[3, 2]
Total Authors: 6
|
| Affiliation: | [1] Univ Sao Paulo, Sao Carlos Inst Chem, Sao Paulo - Brazil
[2] Univ Calif San Diego, Div Trauma Crit Care Burns & Acute Care Surg, Sch Med, Dept Surg, La Jolla, CA 92093 - USA
[3] Univ Calif San Diego, Sch Med, Dept Neurosci, La Jolla, CA 92093 - USA
Total Affiliations: 3
|
| Document type: | Journal article |
| Source: | CELL STRESS & CHAPERONES; v. 26, n. 4, p. 671-684, JUL 2021. |
| Web of Science Citations: | 0 |
| Abstract | |
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. (AU) | |
| FAPESP's process: | 17/26131-5 - The chaperome: study of the relationship of the structure of its components and the maintenance of proteostasis |
| Grantee: | Carlos Henrique Inacio Ramos |
| Support Opportunities: | Research Projects - Thematic Grants |
| FAPESP's process: | 14/16646-0 - Human mortalin: interaction with co-chaperones, p53 and mutants, aggregation kinectics, regulation/modulation and vesicle secretion |
| Grantee: | Paulo Roberto das Dores da Silva |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 12/50161-8 - Study of the structure and function of the Hsp90 chaperone with emphasis on its role in cellular homeostasis |
| Grantee: | Carlos Henrique Inacio Ramos |
| Support Opportunities: | Research Projects - Thematic Grants |
| FAPESP's process: | 17/07335-9 - Studies of human HSP70 isoforms residing in the cytoplasm and mitochondria and their high molecular weight oligomers: interaction with co-chaperones and client proteins |
| Grantee: | Julio Cesar Borges |
| Support Opportunities: | Regular Research Grants |
| FAPESP's process: | 16/22477-1 - Human mortalin: interaction with liposomes, mitochondrion membrane, beta-amyloids and effect of their presence in the toxicity of beta-amyloids on neurons |
| Grantee: | Paulo Roberto das Dores da Silva |
| Support Opportunities: | Scholarships abroad - Research Internship - Post-doctor |