Heat-induced nuclear accumulation of hsc70s is regulated by phosphorylation and inhibited in confluent cells.
Chu
A
A
Department of Physiology, McGill University, Montreal, PQ H3G 1Y6, Canada. achu@med.mcgill.ca
Matusiewicz
N
N
Stochaj
U
U
D021581:Active Transport, Cell Nucleus; D002450:Cell Communication; D002451:Cell Compartmentation; D002467:Cell Nucleus / Q000378:metabolism*; D000431:Ethanol / Q000494:pharmacology; D050883:HSC70 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006367:HeLa Cells; D006801:Humans; D008954:Models, Biological; D009687:Nuclear Proteins / Q000378:metabolism*; D009997:Osmotic Pressure; D010749:Phosphoprotein Phosphatases / Q000037:antagonists & inhibitors; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors; D011505:Protein-Tyrosine Kinases / Q000037:antagonists & inhibitors; D019893:Ribosomal Protein S6 Kinases / Q000037:antagonists & inhibitors
D050883:HSC70 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; C494371:HSPA8 protein, human; D009687:Nuclear Proteins; D000431:Ethanol; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases; D019893:Ribosomal Protein S6 Kinases; D010749:Phosphoprotein Phosphatases