| pubmed-article:16288922 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C0096069 | lld:lifeskim |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C0752312 | lld:lifeskim |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C1370600 | lld:lifeskim |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C1366882 | lld:lifeskim |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C1414184 | lld:lifeskim |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:16288922 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:16288922 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:16288922 | pubmed:dateCreated | 2005-12-12 | lld:pubmed |
| pubmed-article:16288922 | pubmed:abstractText | PAC-1 is an inducible, nuclear-specific, dual-specificity mitogen-activated protein (MAP) kinase phosphatase that has been shown recently to be a transcription target of the human tumor-suppressor protein p53 in signaling apoptosis and growth suppression. However, its substrate specificity and regulation of catalytic activity thus far remain elusive. Here, we report in vitro characterization of PAC-1 phosphatase activity with three distinct MAP kinase subfamilies. We show that the recombinant PAC-1 exists in a virtually inactive state when alone in vitro, and dephosphorylates extracellular signal-regulated kinase 2 (ERK2) but not p38alpha or c-Jun NH(2)-terminal kinase 2 (JNK2). ERK2 dephosphorylation by PAC-1 requires association of its amino-terminal domain with ERK2 that results in catalytic activation of the phosphatase. p38alpha also interacts with but does not activate PAC-1, whereas JNK2 does not bind to or cause catalytic activation by PAC-1. Moreover, our structure-based analysis reveals that individual mutation of the conserved Arg294 and Arg295 that likely comprise the phosphothreonine-binding pocket in PAC-1 to either alanine or lysine results in a nearly complete loss of its phosphatase activity even in the presence of ERK2. These results suggest that Arg294 and Arg295 play an important role in PAC-1 catalytic activation induced by ERK2 binding. | lld:pubmed |
| pubmed-article:16288922 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16288922 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16288922 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16288922 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16288922 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:16288922 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16288922 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16288922 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16288922 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16288922 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16288922 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16288922 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16288922 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:16288922 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:16288922 | pubmed:author | pubmed-author:ZhangQiangQ | lld:pubmed |
| pubmed-article:16288922 | pubmed:author | pubmed-author:FarooqAmjadA | lld:pubmed |
| pubmed-article:16288922 | pubmed:author | pubmed-author:ZhouMing-Ming... | lld:pubmed |
| pubmed-article:16288922 | pubmed:author | pubmed-author:ZengLeiL | lld:pubmed |
| pubmed-article:16288922 | pubmed:author | pubmed-author:MullerMichael... | lld:pubmed |
| pubmed-article:16288922 | pubmed:author | pubmed-author:ChenCan HaoCH | lld:pubmed |
| pubmed-article:16288922 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16288922 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:16288922 | pubmed:volume | 354 | lld:pubmed |
| pubmed-article:16288922 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16288922 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16288922 | pubmed:pagination | 777-88 | lld:pubmed |
| pubmed-article:16288922 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:16288922 | pubmed:meshHeading | pubmed-meshheading:16288922... | lld:pubmed |
| pubmed-article:16288922 | pubmed:meshHeading | pubmed-meshheading:16288922... | lld:pubmed |
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| pubmed-article:16288922 | pubmed:meshHeading | pubmed-meshheading:16288922... | lld:pubmed |
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| pubmed-article:16288922 | pubmed:meshHeading | pubmed-meshheading:16288922... | lld:pubmed |
| pubmed-article:16288922 | pubmed:meshHeading | pubmed-meshheading:16288922... | lld:pubmed |
| pubmed-article:16288922 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16288922 | pubmed:articleTitle | New insights into the catalytic activation of the MAPK phosphatase PAC-1 induced by its substrate MAPK ERK2 binding. | lld:pubmed |
| pubmed-article:16288922 | pubmed:affiliation | Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York University, One Gustave L. Levy Place, New York, NY 10029, USA. | lld:pubmed |
| pubmed-article:16288922 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16288922 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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