EPIDERMAL GROWTH-FACTOR INDUCES SERINE PHOSPHORYLATION OF STATHMIN IN A HUMAN COLON-CARCINOMA CELL-LINE (LIM-1215)
Details
Publication Year 1993-06-25,Volume 268,Issue #18,Page 13396-13405
Journal Title
JOURNAL OF BIOLOGICAL CHEMISTRY
Publication Type
Journal Article
Abstract
Changes in protein phosphorylation in the human colon carcinoma cell line LIM 1215 after stimulation with epidermal growth factor (EGF) have been analyzed by two-dimensional gel electrophoresis and phosphoamino acid analysis. In addition to a number of tyrosine-phosphorylated proteins, a family of small proteins (M(r) 19,000-20,000) is maximally phosphorylated on serine within 5 min of EGF stimulation. One member of the family has been purified by a combination of two-dimensional electrophoresis and reversed-phase high performance liquid chromatography and identified by amino acid sequence analysis as stathmin. Although phosphorylation of stathmin has been reported previously in leukemia cells and following stimulation of hemopoietic or lymphoid cells with several mitogenic agents, this is the first report of stathmin phosphorylation in response to EGF.
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Keywords
NEURON-ENRICHED PHOSPHOPROTEIN; RECEPTOR TYROSINE KINASES; PROTEIN-KINASE; SIGNAL TRANSDUCTION; MONOCLONAL-ANTIBODIES; EGF RECEPTOR; FACTOR-ALPHA; A431 CELLS; IDENTIFICATION; ACTIVATION
Terms of Use/Rights Notice
Refer to copyright notice on published article.


Creation Date: 1993-06-25 12:00:00
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