TY - JOUR
T1 - Shc phosphorylation in myeloid cells is regulated by granulocyte macrophage colony-stimulating factor, interleukin-3, and steel factor and is constitutively increased by p210BCR/ABL
AU - Matsuguchi, Tetsuya
AU - Salgia, Ravi
AU - Hallek, Michael
AU - Eder, Matthias
AU - Druker, Brian
AU - Ernst, Timothy J.
AU - Griffin, James D.
PY - 1994/2/18
Y1 - 1994/2/18
N2 - Granulocyte macrophage colony-stimulating factor, interleukin-3, and steel factor induce proliferation of hematopoietic cells through binding to specific, high affinity, cell surface receptors. However, little is known about post-receptor signal transduction pathways. Here we report that an SH2 domain containing protein previously implicated in the activation of p21ras, Shc, is transiently tyrosine phosphorylated in myeloid cells after stimulation with granulocyte macrophage colonystimulating factor, interleukin-3, or steel factor. Also, She was found to be constitutively tyrosine phosphorylated in myeloid cell lines made factor independent by expression of p210BCR/ABL. A Shc-associated 140-kDa protein was identified, which was phosphorylated on tyrosine residues transiently after cytokine stimulation and constitutively after expression of p210BCR/ABL. These findings suggest that Shc could play an important role in a signal transduction pathway, which leads to the proliferation of myeloid cells.
AB - Granulocyte macrophage colony-stimulating factor, interleukin-3, and steel factor induce proliferation of hematopoietic cells through binding to specific, high affinity, cell surface receptors. However, little is known about post-receptor signal transduction pathways. Here we report that an SH2 domain containing protein previously implicated in the activation of p21ras, Shc, is transiently tyrosine phosphorylated in myeloid cells after stimulation with granulocyte macrophage colonystimulating factor, interleukin-3, or steel factor. Also, She was found to be constitutively tyrosine phosphorylated in myeloid cell lines made factor independent by expression of p210BCR/ABL. A Shc-associated 140-kDa protein was identified, which was phosphorylated on tyrosine residues transiently after cytokine stimulation and constitutively after expression of p210BCR/ABL. These findings suggest that Shc could play an important role in a signal transduction pathway, which leads to the proliferation of myeloid cells.
UR - http://www.scopus.com/inward/record.url?scp=0027939947&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0027939947&partnerID=8YFLogxK
M3 - Article
C2 - 7508932
AN - SCOPUS:0027939947
SN - 0021-9258
VL - 269
SP - 5016
EP - 5021
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 7
ER -