| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 277, Issue 19, 17359-17366, May 10, 2002
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
From the The STAT proteins are a family of latent
transcription factors that are activated by a wide variety of
cytokines. Upon receptor engagement, STATs become tyrosine
phosphorylated, translocate to the nucleus, and induce expression of
target genes. In addition to tyrosine phosphorylation, maximal
activation of some STAT proteins requires serine phosphorylation within
the transactivation domain. Here we focus on STAT phosphorylation after
engagement of the erythropoietin receptor (EPO-R). In Ba/F3-EPO-R
cells, EPO induces tyrosine and serine phosphorylation of STAT1, STAT3,
STAT5A, and STAT5B. Identical regions of the EPO-R couple to both
tyrosine and serine phosphorylation of each cognate STAT protein. A
proximal region of the EPO-R lacking cytoplasmic tyrosines couples to
STAT1 and STAT3 phosphorylation as well as ERK and p38HOG
activation, but not JNK/SAPK. STAT1 serine phosphorylation was perturbed by inhibition of ERK and p38 pathways, whereas only inhibition of ERK activation blocked STAT3 serine phosphorylation in
response to EPO. STAT5A/B phosphorylation is downstream of EPO-R
Tyr343, however, STAT5A/B serine phosphorylation is
unaffected by either ERK or p38 inhibition. Physiological responses
induced by EPO may depend on regulation of serine phosphorylation of
the STAT molecules by p38HOG and the ERK family of kinases
as well as additional serine/threonine kinases.
Regulation of Erythropoietin-induced STAT Serine Phosphorylation
by Distinct Mitogen-activated Protein Kinases*
§¶,
,,§**, and§§¶¶
Institute of Medical Science,
Department of Medical Biophysics and
§§ Laboratory Medicine and Pathobiology,
University of Toronto, and § Ontario Cancer Institute,
Toronto, Ontario M5G 2M9, Canada and ** The Cross Cancer
Institute, Edmonton, Alberta T6G 1Z2, Canada
*
This work was supported in part by Leukemia Research Fund
(to B. W. Z.) and Canadian Institutes of Health Research
Grants 13612 (to D. L. B.) and MOP-36482 (to B. W. Z.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence may be addressed.
¶¶
National Cancer Institute of Canada Research Scientist.
To whom correspondence may be addressed: Ontario Cancer Institute, 610 University Ave., Toronto, Ontario M5G 2M9, Canada. Tel.: 416-946-4455; Fax: 416-946-2065; E-mail: dbarber@uhnres.utoronto.ca.
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  S. Ni, C. Zhao, G.-S. Feng, R. F. Paulson, and P. H. Correll A Novel Stat3 Binding Motif in Gab2 Mediates Transformation of Primary Hematopoietic Cells by the Stk/Ron Receptor Tyrosine Kinase in Response to Friend Virus Infection Mol. Cell. Biol., May 15, 2007; 27(10): 3708 - 3715. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. P. Menon, J. Fang, and D. M. Wojchowski Core erythropoietin receptor signals for late erythroblast development Blood, April 1, 2006; 107(7): 2662 - 2672. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Um and H. F. Lodish Antiapoptotic Effects of Erythropoietin in Differentiated Neuroblastoma SH-SY5Y Cells Require Activation of Both the STAT5 and AKT Signaling Pathways J. Biol. Chem., March 3, 2006; 281(9): 5648 - 5656. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
W. Komyod, U.-M. Bauer, P. C. Heinrich, S. Haan, and I. Behrmann Are STATS Arginine-methylated? J. Biol. Chem., June 10, 2005; 280(23): 21700 - 21705. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Halupa, M. L. Bailey, K. Huang, N. N. Iscove, D. E. Levy, and D. L. Barber A novel role for STAT1 in regulating murine erythropoiesis: deletion of STAT1 results in overall reduction of erythroid progenitors and alters their distribution Blood, January 15, 2005; 105(2): 552 - 561. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
L. S. Argetsinger, J.-L. K. Kouadio, H. Steen, A. Stensballe, O. N. Jensen, and C. Carter-Su Autophosphorylation of JAK2 on Tyrosines 221 and 570 Regulates Its Activity Mol. Cell. Biol., June 1, 2004; 24(11): 4955 - 4967. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. K. H. Lo and Y. H. Wong Signal Transducer and Activator of Transcription 3 Activation by the {delta}-Opioid Receptor via G{alpha}14 Involves Multiple Intermediates Mol. Pharmacol., June 1, 2004; 65(6): 1427 - 1439. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C.-S. Shi and J. H. Kehrl Pyk2 Amplifies Epidermal Growth Factor and c-Src-induced Stat3 Activation J. Biol. Chem., April 23, 2004; 279(17): 17224 - 17231. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. J. Gu, K. Gathy, L. Santiago, E. Chen, M. Huang, L. M. Graves, and B. S. Mitchell Induction of apoptosis in IL-3-dependent hematopoietic cell lines by guanine nucleotide depletion Blood, June 15, 2003; 101(12): 4958 - 4965. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
V. S. Cull, P. A. Tilbrook, E. J. Bartlett, N. L. Brekalo, and C. M. James Type I interferon differential therapy for erythroleukemia: specificity of STAT activation Blood, April 1, 2003; 101(7): 2727 - 2735. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
