Open Access
Article
Src kinases in G-CSF receptor signaling
Matthew Sampson1,Quan-Sheng Zhu1,Seth J Corey1
1
Department of Pediatrics, Children's Hospital of Philadelphia, USA
DOI: 10.2741/2160 Volume 12 Issue 4, pp.1463-1474
Published: 01 January 2007
Abstract

The Granulocyte Colony-Stimulating Factor (G-CSF) receptor, a member of the hematopoietin cytokine receptor superfamily, functions as a homodimer and requires the recruitment of cytosolic protein tyrosine kinases (PTKs) to transduce its signal. At least two cytosolic PTKs are primarily involved: Jak2, a member of the Janus family, and Lyn, a member of the Src family. Through poorly understood mechanisms, these kinases functionally interact with the G-CSF receptor. Jak2 primarily enlists members of the signal transducer and activator of transcription (STAT) family and Lyn phosphorylates a number of adaptor molecules, which link the G-CSF receptor to phosphatidylinositol (PI) 3'-kinase and extracellular signal-regulated kinases (Erk) pathways. This review presents evidence that the Src kinases play a major role in the pathways of G-CSF-mediated proliferation, survival, and differentiation. Identification of Src-dependent pathways provides drug targets useful in the treatment of myeloid leukemias.

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Matthew Sampson, Quan-Sheng Zhu, Seth J Corey. Src kinases in G-CSF receptor signaling. Frontiers in Bioscience-Landmark. 2007. 12(4); 1463-1474.