Abstract
Wolf et al . have identified a new member of the growing Gab family of docking proteins, termed Gab3. Gab3 transcripts are expressed in greater amounts in spleen and thymus than in other organs, which suggested that Gab3 may have an important role in immune cell-specific signaling. Gab3 associated with the Src homology 2 (SH2) domain-containing protein tyrosine phosphatase (SHP2) and the 85-kD subunit of phosphatidylinositol 3-kinase (p85), and Gab3 became phosphorylated on tyrosine residues in cells treated with macrophage-colony-stimulating factor (M-CSF). "Pull-down" assays consisting of chimeric proteins comprising glutathione S -transferase (GST) and various SH3 domains indicated that Gab3 could interact with the SH3 domains from Grb2 and from Src, Fyn, Lyn, suggesting that one or more of these protein tyrosine kinases may phosphorylate Gab3. The amount of Gab3 mRNA (but not that of Gab2 mRNA) increased greatly after M-CSF treatment of cells expressing Fms (the receptor for M-CSF). Gab3 may participate in regulating the morphological differentiation of cells into macrophages, as overexpression of Gab3 directed immature cells into the macrophage pathway. I. Wolf, B. J. Jenkins, Y. Liu, M. Seiffert, J. M. Custodio, P. Young, L. R. Rohrschneider, Gab3, a new DOS/Gab family member, facilitates macrophage differentiation. Mol. Cell. Biol. 22 , 231-244 (2002). [Abstract] [Full Text]
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