Medical implications of understanding the functions of human small heat shock proteins.
Small heat shock proteins (sHsps) are ubiquitous molecular chaperones that are implicated in a variety of diseases. Upon stress, they stabilize unfolding proteins and prevent them from aggregating. However, under physiological conditions without severe stress, some sHsps interact with other proteins. In a perspective view, their ability to bind specific client proteins might allow them to fine-tune the availability of the client for other, client-dependent cellular processes. Additionally, some sHsps seem to interact with specific co-chaperones. These co-chaperones are usually part of large protein machineries that are functionally modulated upon sHsps interaction. Finally, secreted human sHsps seem to interact with receptor proteins, potentially as signal molecules transmitting the stress status from one cell to another. This review focuses on the mechanistic description of these different binding modes for human sHsps and how this might help to understand and modulate the function of sHsps in the context of disease.
Department Chemie, Technische Universität München, D-85747 Garching, Germany.
Evgeny V
EV
Mymrikov
Martin
M
Haslbeck
D000818:Animals; D015510:Clinical Medicine; D050888:Heat-Shock Proteins, Small / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D013312:Stress, Physiological
D050888:Heat-Shock Proteins, Small
molecular chaperone; protein aggregation; protein folding; protein homeostasis; protein–protein interaction; small heat shock protein; α-crystallin