HSPB1, actin filament dynamics, and aging cells.
Investigations into the possible roles of human HSPB1 in aging have focused on its role as a molecular chaperone protecting partially folded or unfolded proteins, particularly during oxidative stress. A thorough analysis of potential roles of HSPB1 in aging cells has been hampered by a limited knowledge of its functions in living cells. Most studies have employed cell-free extracts and purified proteins. For example, HSPB1 is known to bind actin in vitro, and this observation led to the hypothesis that HSPB1 regulates actin filament dynamics. In the study summarized herein, the role of HSPB1 in regulating actin filament dynamics was further investigated by using cultured human cells. These results show that HSPB1 and actin form a complex in vivo and that HSPB1 is important for cell motility. A model for HSPB1 as a regulator of actin filament dynamics is presented, and evidence from the literature on cytoskeletal alterations in aging cells is discussed.
Department of Molecular and Cell Biology, University of Connecticut, Storrs, Connecticut, USA.
Bindi M
BM
Doshi
Lawrence E
LE
Hightower
Juliet
J
Lee
D008841:Actin Cytoskeleton / Q000378:metabolism*; D000199:Actins / Q000378:metabolism* / Q000502:physiology; D002465:Cell Movement / Q000502:physiology*; D002478:Cells, Cultured; D016922:Cellular Senescence; D003599:Cytoskeleton / Q000378:metabolism; D055551:HSP27 Heat-Shock Proteins / Q000235:genetics / Q000378:metabolism*; D006360:Heat-Shock Proteins; D006801:Humans; D018832:Molecular Chaperones / Q000378:metabolism; D018384:Oxidative Stress
D000199:Actins; D055551:HSP27 Heat-Shock Proteins; C057725:HSPB1 protein, human; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones