Heat shock proteins and the biogenesis of cellular membranes.

作者: Antonio De Maio , Lawrence E. Hightower

DOI: 10.1007/S12192-020-01173-2

关键词:

摘要: The successful function of cells is importantly contributed by lipid membranes that are more than a simple physical barrier. major components cellular lipids, in particular glycerophospholipids, have the capacity to assemble spontaneously into vesicles containing bilayer after exposure an aqueous milieu due their amphiphilic characteristics. form and encapsulate substrates has been proposed as fundamental event during biogenesis cells. However, stability small compromised expansion larger complex particles. Recent observations (Cornell et al. Proc Natl Acad Sci U S A 116:17239-17244, 2019) shown insertion amino acids rudimentary could play stabilizing role was critical formation early Fatty were likely substituted glycerophospholipids replaced polypeptides evolution protocells. Thus, archaic peptides displaying lipid-binding membrane-penetrating capacities played key development current In this regard, heat shock proteins (HSP), particularly Hsp70 (HSPA) HSP (HSPB) families, portrayed role. Indeed, bacterial DnaK closest sequence earliest members family inserts spontaneously. Moreover, extensive studies Vigh group that, certainly, Hsp70s stabilize membranes. ability ancestral HSP70s HSPs associate with lipids genesis

参考文章(30)
Daniel Segré, Dafna Ben-Eli, David W. Deamer, Doron Lancet, The lipid world. Origins of Life and Evolution of Biospheres. ,vol. 31, pp. 119- 145 ,(2001) , 10.1023/A:1006746807104
Virginia L. Vega, Monica Rodríguez-Silva, Tiffany Frey, Mathias Gehrmann, Juan Carlos Diaz, Claudia Steinem, Gabriele Multhoff, Nelson Arispe, Antonio De Maio, Hsp70 Translocates into the Plasma Membrane after Stress and Is Released into the Extracellular Environment in a Membrane-Associated Form that Activates Macrophages Journal of Immunology. ,vol. 180, pp. 4299- 4307 ,(2008) , 10.4049/JIMMUNOL.180.6.4299
Nelson Arispe, Antonio De Maio, ATP and ADP Modulate a Cation Channel Formed by Hsc70 in Acidic Phospholipid Membranes Journal of Biological Chemistry. ,vol. 275, pp. 30839- 30843 ,(2000) , 10.1074/JBC.M005226200
Stephen H White, William C Wimley, Hydrophobic interactions of peptides with membrane interfaces. Biochimica et Biophysica Acta. ,vol. 1376, pp. 339- 352 ,(1998) , 10.1016/S0304-4157(98)00021-5
Gabrielle Armijo, Jonathan Okerblom, David M. Cauvi, Victor Lopez, Diana E. Schlamadinger, Judy Kim, Nelson Arispe, Antonio De Maio, Interaction of heat shock protein 70 with membranes depends on the lipid environment Cell Stress & Chaperones. ,vol. 19, pp. 877- 886 ,(2014) , 10.1007/S12192-014-0511-X
Nelson Arispe, Michael Doh, Olga Simakova, Boris Kurganov, Antonio De Maio, Hsc70 and Hsp70 interact with phosphatidylserine on the surface of PC12 cells resulting in a decrease of viability The FASEB Journal. ,vol. 18, pp. 1636- 1645 ,(2004) , 10.1096/FJ.04-2088COM
Thomas Kirkegaard, Anke G. Roth, Nikolaj H. T. Petersen, Ajay K. Mahalka, Ole Dines Olsen, Irina Moilanen, Alicja Zylicz, Jens Knudsen, Konrad Sandhoff, Christoph Arenz, Paavo K. J. Kinnunen, Jesper Nylandsted, Marja Jäättelä, Hsp70 stabilizes lysosomes and reverts Niemann–Pick disease-associated lysosomal pathology Nature. ,vol. 463, pp. 549- 553 ,(2010) , 10.1038/NATURE08710
C Tanford, The hydrophobic effect and the organization of living matter Science. ,vol. 200, pp. 1012- 1018 ,(1978) , 10.1126/SCIENCE.653353