ATP induces dissociation of the 90 kDa heat shock protein (hsp90) from F-actin: interference with the binding of heavy meromyosin.
The 90 kDa heat shock protein (hsp90) is a major cytoplasmic molecular chaperone associating with various other proteins such as steroid receptors, protein kinases and filamentous actin. hsp90 has also been shown to bind ATP, which causes a conformational change of the protein. The physiological role and significance of ATP binding by hsp90, however, has remained unclear. Here we show through direct, microscopic observations, that ATP induces the dissociation of actin filaments from immobilized molecules of hsp90 as well as the dissociation of F-actin from heavy meromyosin in the presence of hsp90.
Kellermayer
M S
MS
Central Research Laboratory, University Medical School of Pécs, Hungary.
Csermely
P
P
D000199:Actins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000494:pharmacology*; D000818:Animals; D005260:Female; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D008099:Liver / Q000378:metabolism; D008297:Male; D051379:Mice; D008815:Mice, Inbred Strains; D008961:Models, Structural; D010920:Placenta / Q000378:metabolism; D011247:Pregnancy; D011485:Protein Binding
D000199:Actins; D018841:HSP90 Heat-Shock Proteins; D000255:Adenosine Triphosphate