scholarly journals MAP Kinase Phosphatase-1 Gene Transcription in Rat Neuroendocrine Cells Is Modulated by a Calcium-sensitive Block to Elongation in the First Exon

2001 ◽  
Vol 276 (36) ◽  
pp. 33319-33327 ◽  
Author(s):  
Stephan Ryser ◽  
Silvia Tortola ◽  
Goedele van Haasteren ◽  
Marco Muda ◽  
Senlin Li ◽  
...  
Keyword(s):  
Map Kinase ◽  
Gene Transcription ◽  
Neuroendocrine Cells ◽  
Map Kinase Phosphatase

scholarly journals MAP Kinase Phosphatase 1 (MKP-1/DUSP1) Is Neuroprotective in Huntington's Disease via Additive Effects of JNK and p38 Inhibition

2013 ◽  
Vol 33 (6) ◽  
pp. 2313-2325 ◽  
Author(s):  
D. M. Taylor ◽  
R. Moser ◽  
E. Regulier ◽  
L. Breuillaud ◽  
M. Dixon ◽  
...  
Keyword(s):  
Huntington's Disease ◽  
Map Kinase ◽  
Huntington’S Disease ◽  
Additive Effects ◽  
Map Kinase Phosphatase

scholarly journals Multiple Regions of MAP Kinase Phosphatase 3 Are Involved in Its Recognition and Activation by ERK2

2000 ◽  
Vol 276 (9) ◽  
pp. 6506-6515 ◽  
Author(s):  
Bo Zhou ◽  
Li Wu ◽  
Kui Shen ◽  
Jialin Zhang ◽  
David S. Lawrence ◽  
...  
Keyword(s):  
Map Kinase ◽  
Map Kinase Phosphatase ◽  
Multiple Regions

Over-expression and refolding of MAP kinase phosphatase 3

2007 ◽  
Vol 54 (2) ◽  
pp. 253-260 ◽  
Author(s):  
John K. Mark ◽  
Sophie Smith ◽  
Mary Alice Hefford
Keyword(s):  
Map Kinase ◽  
Over Expression ◽  
Map Kinase Phosphatase

scholarly journals Histone H3 as a novel substrate for MAP kinase phosphatase-1

2009 ◽  
Vol 296 (2) ◽  
pp. C242-C249 ◽  
Author(s):  
Corttrell M. Kinney ◽  
Unni M. Chandrasekharan ◽  
Lin Yang ◽  
Jianzhong Shen ◽  
Michael Kinter ◽  
...  
Keyword(s):  
Map Kinase ◽  
Map Kinases ◽  
Histone H3 ◽  
Dual Specificity ◽  
Map Kinase Phosphatase ◽  
Mitogen Activated Protein ◽  
And Control ◽  
Interfering Rna ◽  
Endothelial Growth Factor

Mitogen-activated protein (MAP) kinase phosphatase-1 (MKP-1) is a nuclear, dual-specificity phosphatase that has been shown to dephosphorylate MAP kinases. We used a “substrate-trap” technique involving a mutation in MKP-1 of the catalytically critical cysteine to a serine residue (“CS” mutant) to capture novel MKP-1 substrates. We transfected the MKP-1 (CS) mutant and control (wild-type, WT) constructs into phorbol 12-myristate 13-acetate (PMA)-activated COS-1 cells. MKP-1-substrate complexes were immunoprecipitated, which yielded four bands of 17, 15, 14, and 10 kDa with the CS MKP-1 mutant but not the WT MKP-1. The bands were identified by mass spectrometry as histones H3, H2B, H2A, and H4, respectively. Histone H3 was phosphorylated, and purified MKP-1 dephosphorylated histone H3 (phospho-Ser-10) in vitro; whereas, histone H3 (phospho-Thr-3) was unaffected. We have previously shown that thrombin and vascular endothelial growth factor (VEGF) upregulated MKP-1 in human endothelial cells (EC). We now show that both thrombin and VEGF caused dephosphorylation of histone H3 (phospho-Ser-10) and histone H3 (phospho-Thr-3) in EC with kinetics consistent with MKP-1 induction. Furthermore, MKP-1-specific small interfering RNA (siRNA) prevented VEGF- and thrombin-induced H3 (phospho-Ser-10) dephosphorylation but had no effect on H3 (phospho-Thr-3 or Thr-11) dephosphorylation. In summary, histone H3 is a novel substrate of MKP-1, and VEGF- and thrombin-induced H3 (phospho-Ser-10) dephosphorylation requires MKP-1. We propose that MKP-1-mediated H3 (phospho-Ser-10) dephosphorylation is a key regulatory step in EC activation by VEGF and thrombin.

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