A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Pim-1 kinase and p100 cooperate to enhance c-myb activity
Tekijät: Leverson JD, Koskinen PJ, Orrico FC, Rainio EM, Jalkanen KJ, Dash AB, Eisenman RN, Ness SA
Kustantaja: CELL PRESS
Julkaisuvuosi: 1998
Journal: Molecular Cell
Tietokannassa oleva lehden nimi: MOLECULAR CELL
Lehden akronyymi: MOL CELL
Vuosikerta: 2
Numero: 4
Aloitussivu: 417
Lopetussivu: 425
Sivujen määrä: 9
ISSN: 1097-2765
DOI: https://doi.org/10.1016/S1097-2765(00)80141-0
Tiivistelmä
The pim-1 oncogene is regulated by hematopoietic cytokine receptors, encodes a serine/threonine protein kinase, and cooperates with c-myc in lymphoid cell transformation. Using a yeast two-hybrid screen, we found that pim-1 protein binds to p100, a transcriptional coactivator that interacts with the c-Myb transcription factor. Pim-1 phosphorylated p100 in vitro, formed a stable complex with p100 in animal cells, and functioned downstream of Ras to stimulate c-Myb transcriptional activity in a p100-dependent manner. Thus, pim-1 and p100 appear to be components of a novel signal transduction pathway affecting c-Myb activity, linking all three to the cytokine-regulated control of hematopoietic cell growth, differentiation, and apoptosis.
The pim-1 oncogene is regulated by hematopoietic cytokine receptors, encodes a serine/threonine protein kinase, and cooperates with c-myc in lymphoid cell transformation. Using a yeast two-hybrid screen, we found that pim-1 protein binds to p100, a transcriptional coactivator that interacts with the c-Myb transcription factor. Pim-1 phosphorylated p100 in vitro, formed a stable complex with p100 in animal cells, and functioned downstream of Ras to stimulate c-Myb transcriptional activity in a p100-dependent manner. Thus, pim-1 and p100 appear to be components of a novel signal transduction pathway affecting c-Myb activity, linking all three to the cytokine-regulated control of hematopoietic cell growth, differentiation, and apoptosis.
Ladattava julkaisu This is an electronic reprint of the original article. |