Is the lipochaperone activity of sHSP a key to the stress response encoded in its primary sequence?

• Published in: Cell stress & chaperones Vol. 28; no. 1; pp. 21 - 33
• Main Authors: Bellanger, Tiffany, Weidmann, Stéphanie
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Science + Business Media 01-01-2023; Springer Netherlands; Springer Nature B.V
• Subjects: Amino Acid Sequence; Amino acids; Biochemistry; Biomedical and Life Sciences; Biomedicine; Cancer Research; Cell Biology; Cell membranes; Fluidity; Heat-Shock Proteins - metabolism; Heat-Shock Proteins, Small - metabolism; Immunology; Lipids; Literature reviews; Membrane fluidity; Membranes; MINI REVIEW; Molecular Chaperones - metabolism; Neurosciences; Oligomerization; Proteins; Residues; Stress proteins; Structure-function relationships; Viscosity; Lipochaperone activity; Small heat shock protein; Stress response; Protein structure
• ISSN: 1355-8145; 1466-1268
• DOI: 10.1007/s12192-022-01308-7

Several strategies have been put in place by organisms to adapt to their environment. One of these strategies is the production of stress proteins such as sHSPs, which have been widely described over the last 30 years for their role as molecular chaperones. Some sHSPs have, in addition, the particularity to exert a lipochaperone role by interacting with membrane lipids to maintain an optimal membrane fluidity. However, the mechanisms involved in this sHSP-lipid interaction remain poorly understood and described rather sporadically in the literature. This review gathers the information concerning the structure and function of these proteins available in the literature in order to highlight the mechanism involved in this interaction. In addition, analysis of primary sequence data of sHSPs available in database shows that sHSPs can interact with lipids via certain amino acid residues present on some β sheets of these proteins. These residues could have a key role in the structure and/or oligomerization dynamics of sHPSs, which is certainly essential for interaction with membrane lipids and consequently for maintaining optimal cell membrane fluidity.