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GM‐CSF induces the tyrosine phosphorylation of three isoforms of shc and its association with GRB2 in TF‐1 cell
Author(s) -
Shi Xiaoqing,
Qin Junchuan,
Zhu Dexu
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201232
Subject(s) - grb2 , phosphorylation , tyrosine phosphorylation , signal transducing adaptor protein , gene isoform , tyrosine , microbiology and biotechnology , chemistry , sh2 domain , signal transduction , protein tyrosine phosphatase , cancer research , biology , biochemistry , gene
Abstract This report demonstrates that GM‐CSF induces the tyrosine phosphorylation of Shc protein which is implicated in Ras activation. Three isoforms of She are ubiqitously phosphorylated induced by GM‐CSF in TF‐1, a cell line of erythroid origin. It is also shown that She is associated with the adaptor protein Grb2. The formation of Shc‐Grb2 complex may directly link tyrosine phosphorylation events to Ras activation in TF‐1 cells.