MKP-8, a novel MAPK phosphatase that inhibits p38 kinase
In: Biochemical and Biophysical Research Communications, Jg. 330 (2005-05-01), S. 511-518
Online
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Zugriff:
Intracellular signaling pathways and their relationship to malignant progression have become a major focus of cancer biology. The dual-specificity phosphatase (DSP) family is a more recently identified family of intracellular signaling modulators. We have identified a novel protein phosphatase with a well-conserved DSP catalytic domain containing the DSP catalytic motif, xHCxxGxSRS, and mitogen-activated protein kinase phosphatase (MKP) motif, AYLM. Because of these unique characteristics, the protein was named mitogen-activated protein kinase phosphatase-8 (MKP-8). This protein is approximately 20 kDa in size and mainly localizes to the nuclear compartment of the cell. MKP-8 is expressed in embryonal cancers (retinoblastoma, neuroepithelioma, and neuroblastoma) and has limited expression in normal tissues. MKP-8 displays significant phosphatase activity that is inhibited by a cysteine to serine substitution in the catalytic domain. When co-expressed with activated MAPKs, MKP-8 is able to inhibit p38 kinase phosphorylation and downstream activity.
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MKP-8, a novel MAPK phosphatase that inhibits p38 kinase
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Autor/in / Beteiligte Person: | Yang, Jianhua ; Burlingame, Susan ; Vasudevan, Sanjeev A. ; Patel, Parul ; Nuchtern, Jed G. ; Lazo, John S. ; Skoko, John J. ; Wang, Kuan |
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Zeitschrift: | Biochemical and Biophysical Research Communications, Jg. 330 (2005-05-01), S. 511-518 |
Veröffentlichung: | Elsevier BV, 2005 |
Medientyp: | unknown |
ISSN: | 0006-291X (print) |
DOI: | 10.1016/j.bbrc.2005.03.028 |
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