Open AccessAssociation of hematopoietic cell phosphatase with c-Kit after stimulation with c-Kit ligand.
Author(s) -
Taolin Yi,
James N. Ihle
Publication year - 1993
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.13.6.3350
Subject(s) - biology , protein tyrosine phosphatase , stem cell factor , phosphorylation , dephosphorylation , phosphatase , sh2 domain , signal transduction , tyrosine phosphorylation , microbiology and biotechnology , hematopoietic growth factor , proto oncogene proteins c kit , haematopoiesis , receptor tyrosine kinase , tyrosine , proto oncogene tyrosine protein kinase src , tyrosine kinase , stem cell , biochemistry
Protein tyrosine phosphorylation and dephosphorylation have been implicated in the growth and functional responses of hematopoietic cells. Recent studies have identified a novel protein tyrosine phosphatase, termed hematopoietic cell phosphatase (HCP) or PTP1C, that is predominantly expressed in hematopoietic cells. HCP encodes a cytoplasmic phosphatase that contains two src homology 2 (SH2) domains. Since SH2 domains have been shown to target the association of signal-transducing molecules with activated growth factor receptors containing intrinsic protein kinase activity, we assessed the association of HCP with two hematopoietic growth factor receptors, c-Kit and c-Fms. The results demonstrate that HCP transiently associates with ligand-activated c-Kit but not c-Fms and that this association occurs through the SH2 domains. In both colony-stimulating factor 1- and stem cell factor-stimulated cells, there is a marginal increase in tyrosine phosphorylation of HCP. Lastly, HCP can dephosphorylate autophosphorylated c-Kit and c-Fms in in vitro reactions. The potential role of HCP in stem cell factor signal transduction is discussed.