TY - JOUR
T1 - Small heat shock proteins
T2 - multifaceted proteins with important implications for life
AU - Carra, Serena
AU - Alberti, Simon
AU - Benesch, Justin L.P.
AU - Boelens, Wilbert
AU - Buchner, Johannes
AU - Carver, John A.
AU - Cecconi, Ciro
AU - Ecroyd, Heath
AU - Gusev, Nikolai
AU - Hightower, Lawrence E.
AU - Klevit, Rachel E.
AU - Lee, Hyun O.
AU - Liberek, Krzysztof
AU - Lockwood, Brent
AU - Poletti, Angelo
AU - Timmerman, Vincent
AU - Toth, Melinda E.
AU - Vierling, Elizabeth
AU - Wu, Tangchun
AU - Tanguay, Robert M.
N1 - Publisher Copyright:
© 2019, Cell Stress Society International.
PY - 2019/3/1
Y1 - 2019/3/1
N2 - Small Heat Shock Proteins (sHSPs) evolved early in the history of life; they are present in archaea, bacteria, and eukaryota. sHSPs belong to the superfamily of molecular chaperones: they are components of the cellular protein quality control machinery and are thought to act as the first line of defense against conditions that endanger the cellular proteome. In plants, sHSPs protect cells against abiotic stresses, providing innovative targets for sustainable agricultural production. In humans, sHSPs (also known as HSPBs) are associated with the development of several neurological diseases. Thus, manipulation of sHSP expression may represent an attractive therapeutic strategy for disease treatment. Experimental evidence demonstrates that enhancing the chaperone function of sHSPs protects against age-related protein conformation diseases, which are characterized by protein aggregation. Moreover, sHSPs can promote longevity and healthy aging in vivo. In addition, sHSPs have been implicated in the prognosis of several types of cancer. Here, sHSP upregulation, by enhancing cellular health, could promote cancer development; on the other hand, their downregulation, by sensitizing cells to external stressors and chemotherapeutics, may have beneficial outcomes. The complexity and diversity of sHSP function and properties and the need to identify their specific clients, as well as their implication in human disease, have been discussed by many of the world’s experts in the sHSP field during a dedicated workshop in Québec City, Canada, on 26–29 August 2018.
AB - Small Heat Shock Proteins (sHSPs) evolved early in the history of life; they are present in archaea, bacteria, and eukaryota. sHSPs belong to the superfamily of molecular chaperones: they are components of the cellular protein quality control machinery and are thought to act as the first line of defense against conditions that endanger the cellular proteome. In plants, sHSPs protect cells against abiotic stresses, providing innovative targets for sustainable agricultural production. In humans, sHSPs (also known as HSPBs) are associated with the development of several neurological diseases. Thus, manipulation of sHSP expression may represent an attractive therapeutic strategy for disease treatment. Experimental evidence demonstrates that enhancing the chaperone function of sHSPs protects against age-related protein conformation diseases, which are characterized by protein aggregation. Moreover, sHSPs can promote longevity and healthy aging in vivo. In addition, sHSPs have been implicated in the prognosis of several types of cancer. Here, sHSP upregulation, by enhancing cellular health, could promote cancer development; on the other hand, their downregulation, by sensitizing cells to external stressors and chemotherapeutics, may have beneficial outcomes. The complexity and diversity of sHSP function and properties and the need to identify their specific clients, as well as their implication in human disease, have been discussed by many of the world’s experts in the sHSP field during a dedicated workshop in Québec City, Canada, on 26–29 August 2018.
KW - Human diseases
KW - Plant biology
KW - Protein quality control
KW - Small heat shock proteins
UR - http://www.scopus.com/inward/record.url?scp=85061656143&partnerID=8YFLogxK
U2 - 10.1007/s12192-019-00979-z
DO - 10.1007/s12192-019-00979-z
M3 - Review article
SN - 1355-8145
VL - 24
SP - 295
EP - 308
JO - Cell Stress and Chaperones
JF - Cell Stress and Chaperones
IS - 2
ER -