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Involvement of the protein tyrosine phosphatase SHP-1 in ras-mediated activation of the mitogen-activated protein kinase pathway

: Krautwald, S.; Büscher, D.; Kummer, V.; Buder, S.; Baccarini, M.

Molecular and Cellular Biology 16 (1996), No.11, pp.5955-5963
ISSN: 0270-7306
Journal Article
Fraunhofer ITA ( ITEM) ()
biochemistry; cell culture; colony stimulating factor; enzyme activation; growth factor; immunology; macrophage; molecular biology; mouse; phosphorylation; protein kinase; signal transduction; tyrosine

Ubiquitously expressed SH2-containing tyrosine phosphatases interact physically with tyrosine kinase receptors or their substrates and relay positive mitogenic signals via the activation of the Ras-mitogen-activated protein kinase (MAPK) pathway. Conversely, the structurally related phosphatase SHP-1 is predominantly expressed in hemopoietic cells and becomes tyrosine phosphorylated upon colony-stimulating factor 1 treatment of macrophages without associating with the colony-stimulating factor 1 receptor tyrosine kinase. Mice lacking functional SHP-1 develop systemic autoimmune disease with accumulation of macrophages, suggesting that SHP-1 may be a negative regulator of hemopoietic cell growth. By using macrophages expressing dominant negative Ras und the me[v]/me[v] mouse mutant, we show that SHP-1 is activated in the course of mitogenic signal transduction in a Ras-dependent manner and that its activity is necessary for the Ras-dependent activation of the MAPK.