Leukemia inhibitory factor promotes Hsp90 association with STAT3 in mouse embryonic stem cells.
Self-renewal of in vitro cultured mouse embryonic stem (mES) cells is dependent on the presence of leukemia inhibitory factor (LIF). LIF induces overexpression and tyrosine phosphorylation of STAT3 (signal transducer and activator of transcription 3) and its subsequent nuclear translocation. The molecular chaperone heat shock protein 90 (Hsp90) is involved in the activation and maturation of a wide variety of substrate proteins. We investigated the effect of LIF withdrawal on the protein expression levels of STAT3 and Hsp90 and on the interactions between STAT3 and Hsp90. Taken together the data presented here suggest that LIF promotes the interaction of Hsp90 with STAT3 during self-renewal, indicating a potentially pivotal role for Hsp90 in the LIF-based maintenance of self-renewal of mouse embryonic stem cells.
Setati
Mokgadi M
MM
Biomedical Biotechnology Research Unit, Department of Biochemistry, Microbiology and Biotechnology, Rhodes University, Grahamstown, South Africa.
Prinsloo
Earl
E
Longshaw
Victoria M
VM
Murray
Patricia A
PA
Edgar
David H
DH
Blatch
Gregory L
GL
D000818:Animals; D015153:Blotting, Western; D002478:Cells, Cultured; D015536:Down-Regulation; D053595:Embryonic Stem Cells / Q000378:metabolism; D005455:Fluorescent Antibody Technique; D018841:HSP90 Heat-Shock Proteins / Q000187:drug effects / Q000378:metabolism*; D018398:Homeodomain Proteins / Q000378:metabolism; D053605:Leukemia Inhibitory Factor / Q000494:pharmacology*; D051379:Mice; D008954:Models, Biological; D000071317:Nanog Homeobox Protein; D050796:STAT3 Transcription Factor / Q000187:drug effects / Q000378:metabolism*; D015398:Signal Transduction
D018841:HSP90 Heat-Shock Proteins; D018398:Homeodomain Proteins; D053605:Leukemia Inhibitory Factor; D000071317:Nanog Homeobox Protein; C475540:Nanog protein, mouse; D050796:STAT3 Transcription Factor