NDLI: Regulation of GATA-2 Phosphorylation by Mitogen-activated Protein Kinase and Interleukin-3

Content Provider	Journal of Biological Chemistry (JBC)
Author	Towatari, Masayuki May, Gillian E. Marais, Richard Perkins, Gordon R. Marshall, Christopher J. Cowley, Sally Enver, Tariq
Abstract	GATA-2 is a member of a family of transcription factors which bind a common DNA sequence motif (WGATAR) through an evolutionarily conserved zinc finger domain. An essential role for GATA-2 in the development of hematopoietic stem cells has recently been shown in gene targeting experiments in mice. Here we show that GATA-2 exists in hematopoietic progenitor cells as a phosphoprotein. Stimulation of progenitors with interleukin-3 (IL-3) results in enhanced phosphorylation of GATA-2 which occurs within 5 min. IL-3 is known to signal in part through mitogen-activated protein (MAP) kinase, and evidence for MAP kinase signaling in the control of GATA-2 phosphorylation was obtained by genetically manipulating the MAP kinase pathway in COS cells using either constitutively activating or interfering mutants of MAP kinase kinase. Furthermore, using an interfering mutant of MAP kinase kinase, we directly demonstrated a critical role for the MAP kinase pathway in the IL-3-dependent phosphorylation of GATA-2 in hematopoietic progenitor cells. Finally, in vitro phosphorylation experiments using recombinant GATA-2 raise the possibility that MAP kinase itself may phosphorylate GATA-2. Our results provide evidence for phosphorylation via the MAP kinase pathway constituting a cytoplasmic link between GATA-2 and growth factor receptors and are consistent with the hypothesis that GATA-2 is involved in the growth factor responsiveness and proliferation control of hematopoietic progenitor cells.
Related Links	http://www.jbc.org/content/270/8/4101.abstract
Ending Page	4107
Starting Page	4101
Page Count	7
File Format	HTM / HTML PDF
ISSN	00219258
Journal	Journal of Biological Chemistry (JBC)
Issue Number	8
Volume Number	270
DOI	10.1074/jbc.270.8.4101
e-ISSN	1083351X
Language	English
Publisher	American Society for Biochemistry and Molecular Biology
Publisher Date	1995-02-24
Access Restriction	Open
Subject Keyword	Cell Biology and Metabolism
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

Molecular Cloning of Mitogen-activated Protein/ERK Kinase Kinases (MEKK) 2 and 3 REGULATION OF SEQUENTIAL PHOSPHORYLATION PATHWAYS INVOLVING MITOGEN-ACTIVATED PROTEIN KINASE AND c-Jun KINASE

Constitutive Activation of Mitogen-activated Protein Kinase-activated Protein Kinase 2 by Mutation of Phosphorylation Sites and an A-helix Motif

Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase.

Phosphoinositide 3-Kinase Regulation of T Cell Receptor-mediated Interleukin-2 Gene Expression in Normal T Cells

Interleukin-2 Receptor ß Thr-450 Phosphorylation Is a Positive Regulator for Receptor Complex Stability and Activation of Signaling Molecules.

Sequential Phosphorylation by Mitogen-activated Protein Kinase and Glycogen Synthase Kinase 3 Represses Transcriptional Activation by Heat Shock Factor-1

Interleukin-4 Induces Activation of Mitogen-activated Protein Kinase and Phosphorylation of Shc in Human Keratinocytes

Characterization of Graf, the GTPase-activating Protein for Rho Associated with Focal Adhesion Kinase PHOSPHORYLATION AND POSSIBLE REGULATION BY MITOGEN-ACTIVATED PROTEIN KINASE

Regulation of Peroxisome Proliferator-activated Receptor γ Activity by Mitogen-activated Protein Kinase

Regulation of GATA-2 Phosphorylation by Mitogen-activated Protein Kinase and Interleukin-3

Similar Documents

Molecular Cloning of Mitogen-activated Protein/ERK Kinase Kinases (MEKK) 2 and 3 REGULATION OF SEQUENTIAL PHOSPHORYLATION PATHWAYS INVOLVING MITOGEN-ACTIVATED PROTEIN KINASE AND c-Jun KINASE

Constitutive Activation of Mitogen-activated Protein Kinase-activated Protein Kinase 2 by Mutation of Phosphorylation Sites and an A-helix Motif

Parallel and independent regulation of interleukin-3 mRNA turnover by phosphatidylinositol 3-kinase and p38 mitogen-activated protein kinase.

Phosphoinositide 3-Kinase Regulation of T Cell Receptor-mediated Interleukin-2 Gene Expression in Normal T Cells

Interleukin-2 Receptor ß Thr-450 Phosphorylation Is a Positive Regulator for Receptor Complex Stability and Activation of Signaling Molecules.

Sequential Phosphorylation by Mitogen-activated Protein Kinase and Glycogen Synthase Kinase 3 Represses Transcriptional Activation by Heat Shock Factor-1

Interleukin-4 Induces Activation of Mitogen-activated Protein Kinase and Phosphorylation of Shc in Human Keratinocytes

Characterization of Graf, the GTPase-activating Protein for Rho Associated with Focal Adhesion Kinase PHOSPHORYLATION AND POSSIBLE REGULATION BY MITOGEN-ACTIVATED PROTEIN KINASE

Regulation of Peroxisome Proliferator-activated Receptor γ Activity by Mitogen-activated Protein Kinase

Regulation of GATA-2 Phosphorylation by Mitogen-activated Protein Kinase and Interleukin-3