|
|
 Previous Article | Table of Contents | Next Article 
Blood, Vol. 93 No. 6 (March 15), 1999:
pp. 1922-1933
A Novel Spliced Form of SH2-Containing Inositol Phosphatase Is
Expressed During Myeloid Development
David M. Lucas and
Larry R. Rohrschneider
From the Fred Hutchinson Cancer Research Center, Seattle, WA.
SH2-containing Inositol Phosphatase (SHIP) is a 145 kD protein
expressed in hematopoietic cells. SHIP is phosphorylated on tyrosine
after receptor binding by several cytokines and has a negative role in
hematopoiesis. We cloned a murine complementary DNA (cDNA) sequence for
an isoform of SHIP with an internal 183 nucleotide deletion, encoding a
protein 61 amino acids shorter than 145 kD SHIP. This deletion
eliminates potential SH3-domain binding regions and a potential binding
site for the p85 subunit of Phosphatidylinositol 3-Kinase. Using
polyclonal anti-SHIP antibodies, we and others have previously observed
a 135 kD SHIP isoform that is coexpressed with 145 kD SHIP. Here, we
used monoclonal antibodies raised against the region deleted in the
spliced form to show that the product of the novel spliced SHIP cDNA is
antigenically identical to the 135 kD SHIP isoform. Like 145 kD SHIP,
135 kD SHIP expression was induced on differentiation of bone marrow cells. After macrophage colony-stimulating factor (M-CSF) stimulation of FDC-P1(Fms) myeloid cells, both 145 and 135 kD SHIP
forms were tyrosine phosphorylated and could be coimmunoprecipitated
with antibodies to Shc and Grb2. However, experiments showed only a weak association of 135 kD SHIP with p85. A potentially analogous 135 kD SHIP species also appears in human differentiated leukocytes.
 CiteULike  Connotea  Del.icio.us  Digg  Reddit  Technorati What's this?
This article has been cited by other articles:
|
|
|
|
 
S. J. Harris, R. V. Parry, J. Westwick, and S. G. Ward
Phosphoinositide Lipid Phosphatases: Natural Regulators of Phosphoinositide 3-Kinase Signaling in T Lymphocytes
J. Biol. Chem.,
February 1, 2008;
283(5):
2465 - 2469.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
A. S. J. Marshall, J. A. Willment, H.-H. Lin, D. L. Williams, S. Gordon, and G. D. Brown
Identification and Characterization of a Novel Human Myeloid Inhibitory C-type Lectin-like Receptor (MICL) That Is Predominantly Expressed on Granulocytes and Monocytes
J. Biol. Chem.,
April 9, 2004;
279(15):
14792 - 14802.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
C. P. Baran, S. Tridandapani, C. D. Helgason, R. K. Humphries, G. Krystal, and C. B. Marsh
The Inositol 5'-Phosphatase SHIP-1 and the Src Kinase Lyn Negatively Regulate Macrophage Colony-stimulating Factor-induced Akt Activity
J. Biol. Chem.,
October 3, 2003;
278(40):
38628 - 38636.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. W. Freeburn, K. L. Wright, S. J. Burgess, E. Astoul, D. A. Cantrell, and S. G. Ward
Evidence That SHIP-1 Contributes to Phosphatidylinositol 3,4,5-Trisphosphate Metabolism in T Lymphocytes and Can Regulate Novel Phosphoinositide 3-Kinase Effectors
J. Immunol.,
November 15, 2002;
169(10):
5441 - 5450.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
I. Wolf, B. J. Jenkins, Y. Liu, M. Seiffert, J. M. Custodio, P. Young, and L. R. Rohrschneider
Gab3, a New DOS/Gab Family Member, Facilitates Macrophage Differentiation
Mol. Cell. Biol.,
January 1, 2002;
22(1):
231 - 244.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Z. Tu, J. M. Ninos, Z. Ma, J.-W. Wang, M. P. Lemos, C. Desponts, T. Ghansah, J. M. Howson, and W. G. Kerr
Embryonic and hematopoietic stem cells express a novel SH2-containing inositol 5'-phosphatase isoform that partners with the Grb2 adapter protein
Blood,
October 1, 2001;
98(7):
2028 - 2038.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
Y. Liu, B. Jenkins, J. L. Shin, and L. R. Rohrschneider
Scaffolding Protein Gab2 Mediates Differentiation Signaling Downstream of Fms Receptor Tyrosine Kinase
Mol. Cell. Biol.,
May 1, 2001;
21(9):
3047 - 3056.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
J. E. Damen, M. D. Ware, J. Kalesnikoff, M. R. Hughes, and G. Krystal
SHIP's C-terminus is essential for its hydrolysis of PIP3 and inhibition of mast cell degranulation
Blood,
March 1, 2001;
97(5):
1343 - 1351.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. J. Aman, S. F. Walk, M. E. March, H.-P. Su, D. J. Carver, and K. S. Ravichandran
Essential Role for the C-Terminal Noncatalytic Region of SHIP in Fcgamma RIIB1-Mediated Inhibitory Signaling
Mol. Cell. Biol.,
May 15, 2000;
20(10):
3576 - 3589.
[Abstract]
[Full Text]
|
|
|
|
|
|
|
L. R. Rohrschneider, J. F. Fuller, I. Wolf, Y. Liu, and D. M. Lucas
Structure, function, and biology of SHIP proteins
Genes & Dev.,
March 1, 2000;
14(5):
505 - 520.
[Full Text]
|
|
|
|
|
|
|
C. D. Helgason, C. P. Kalberer, J. E. Damen, S. M. Chappel, N. Pineault, G. Krystal, and R. K. Humphries
A Dual Role for Src Homology 2 Domain-containing Inositol-5-Phosphatase (SHIP) in Immunity: Aberrant Development and Enhanced Function of B Lymphocytes in SHIP-/- Mice
J. Exp. Med.,
February 28, 2000;
191(5):
781 - 794.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Sattler, S. Verma, C. H. Byrne, G. Shrikhande, T. Winkler, P. A. Algate, L. R. Rohrschneider, and J. D. Griffin
BCR/ABL Directly Inhibits Expression of SHIP, an SH2-Containing Polyinositol-5-Phosphatase Involved in the Regulation of Hematopoiesis
Mol. Cell. Biol.,
November 1, 1999;
19(11):
7473 - 7480.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. E. March, D. M. Lucas, M. J. Aman, and K. S. Ravichandran
p135 Src Homology 2 Domain-containing Inositol 5'-Phosphatase (SHIPbeta ) Isoform Can Substitute for p145 SHIP in Fcgamma RIIB1-mediated Inhibitory Signaling in B Cells
J. Biol. Chem.,
September 22, 2000;
275(39):
29960 - 29967.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
M. Sattler, S. Verma, Y. B. Pride, R. Salgia, L. R. Rohrschneider, and J. D. Griffin
SHIP1, an SH2 Domain Containing Polyinositol-5-phosphatase, Regulates Migration through Two Critical Tyrosine Residues and Forms a Novel Signaling Complex with DOK1 and CRKL
J. Biol. Chem.,
January 19, 2001;
276(4):
2451 - 2458.
[Abstract]
[Full Text]
[PDF]
|
|
|
| |
