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Purification and molecular cloning of SH2- and SH3-containing inositol
polyphosphate-5-phosphatase, which is involved in the signaling pathway of
granulocyte-macrophage colony-stimulating factor, erythropoietin, and
Bcr-Abl
H Odai, K Sasaki, A Iwamatsu, T Nakamoto, H Ueno, T Yamagata, K Mitani, Y Yazaki and H Hirai
Third Department of Internal Medicine, Faculty of Medicine, University of
Tokyo, Bunyo-ku, Japan.
Grb2/Ash and Shc are the adapter proteins that link tyrosine-kinase
receptors to Ras and make tyrosine-kinase functionally associated with
receptors and Ras in fibroblasts and hematopoietic cells. Grb2/Ash and Shc
have the SH3, SH2, or phosphotyrosine binding domains. These domains bind
to proteins containing proline-rich regions or tyrosine- phosphorylated
proteins and contribute to the association of Grb2/Ash and Shc with other
signaling molecules. However, there could remain unidentified signaling
molecules that physically and functionally interact with these adapter
proteins and have biologically important roles in the signaling pathways.
By using the GST fusion protein including the full length of Grb2/Ash, we
have found that c-Cbl and an unidentified 135-kD protein (pp135) are
associated with Grb2/Ash. We have also found that they become
tyrosine-phosphorylated by treatment of a human leukemia cell line, UT-7,
with granulocyte-macrophage colony- stimulating factor (GM-CSF). We have
purified the pp135 by using GST- Grb2/Ash affinity column and have isolated
the full-length complementary DNA (cDNA) encoding the pp135 using a cDNA
probe, which was obtained by the degenerate polymerase chain reaction based
on a peptide sequence of the purified pp135. The cloned cDNA has 3,958
nucleotides that contain a single long open reading frame of 3,567
nucleotides, encoding a 1,189 amino acid protein with a predicted molecular
weight of approximately 133 kD. The deduced amino acid sequence reveals
that pp135 is a protein that has one SH2, one SH3, and one proline-rich
domain. The pp135, which contains two motifs conserved among the inositol
polyphosphate-5-phosphatase proteins, was shown to have the inositol
polyphosphate-5-phosphatase activity. The pp135 was revealed to associate
constitutively with Grb2/Ash and inducibly with Shc using UT-7 cells
stimulated with GM-CSF. In the cell lines derived from human chronic
myelogenous leukemia, pp135 was constitutively tyrosine-phosphorylated and
associated with Shc and Bcr-Abl. These facts suggest that pp135 is a
signaling molecule that has a unique enzymatic activity and should play an
important role in the signaling pathway triggered by GM-CSF and in the
transformation of hematopoietic cells caused by Bcr-Abl.
Volume 89,
Issue 8,
pp. 2745-2756,
04/15/1997
Copyright © 1997 by The American Society of Hematology
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