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Down‐regulation but not phosphorylation of stathmin is associated with induction of HL60 cell growth arrest and differentiation by physiological agents
Author(s) -
Johnson W.Eustace B.,
Jones Neil A.,
Rowlands David C.,
Williams Ann,
Guest Simon S.,
Brown Geoffrey
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00416-7
Subject(s) - stathmin , phosphorylation , microbiology and biotechnology , phosphoprotein , hl60 , cellular differentiation , retinoic acid , cell growth , biology , chemistry , cell , cell culture , biochemistry , gene , genetics
Stathmin is a cytosolic phosphoprotein that has an important but, as yet, undefined role in cell proliferation and differentiation. Induction of growth arrest and differentiation of HL60 cells to monocytes by phorbol 12‐myristate 13‐acetate is associated with rapid phosphorylation of the protein. Stathmin phosphorylation was not seen when HL60 cells were induced to differentiate to monocytes, by 1α,25‐dihydroxyvitamin D3, and to neutrophils, by all‐trans retinoic acid and granulocyte colony stimulating factor. In all the above instances, stathmin expression was down‐regulated. Thus, increased stathmin phosphorylation is not required for cell growth arrest or differentiation or down‐regulation of stathmin expression.