| pubmed-article:11948398 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11948398 | lifeskim:mentions | umls-concept:C0162508 | lld:lifeskim |
| pubmed-article:11948398 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:11948398 | lifeskim:mentions | umls-concept:C0248813 | lld:lifeskim |
| pubmed-article:11948398 | lifeskim:mentions | umls-concept:C0258823 | lld:lifeskim |
| pubmed-article:11948398 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:11948398 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:11948398 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:11948398 | pubmed:dateCreated | 2002-4-11 | lld:pubmed |
| pubmed-article:11948398 | pubmed:abstractText | Protein kinase D (PKD), a downstream effector of protein kinase C (PKC), is implicated in suppression of the c-Jun N-terminal kinase (JNK) signaling pathway, however, its mechanism of action is unclear. Transphosphorylation of the PKD activation loop at serines 744/748 by a PKC mediated signal transduction pathway enhances its catalytic activity. Here we show that PKD activation loop phosphorylation at serines 744/748 via PKC, or mutation of these serines to glutamic acid (PKD-S744/748E) also results in complex formation with JNK, indicating that suppression of JNK signaling by PKD involves a direct interaction with JNK. Because catalytically active PKD associates with JNK we determined whether it could phosphorylate the c-Jun N-terminus as a potential mechanism by which it suppresses c-Jun Ser 63 phosphorylation when it complexes with JNK. Purified human PKD and either wild-type PKD from phorbol 12, 13-dibutyrate (PDB)-stimulated cells or unstimulated constitutively active PKD (PKD-S744/748E), phosphorylated the c-Jun N-terminus between amino acids 1-89 at sites distinct from those phosphorylated by JNK. These results demonstrate, for the first time, phosphorylation dependent association of PKD with another signaling molecule and reveal a potential mechanism by which PKD could modulate the ability of JNK to phosphorylate c-Jun by phosphorylating alternative sites in the c-Jun N-terminus when it is complexed with JNK. | lld:pubmed |
| pubmed-article:11948398 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11948398 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11948398 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11948398 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11948398 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11948398 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11948398 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11948398 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11948398 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11948398 | pubmed:issn | 0950-9232 | lld:pubmed |
| pubmed-article:11948398 | pubmed:author | pubmed-author:WaldronRichar... | lld:pubmed |
| pubmed-article:11948398 | pubmed:author | pubmed-author:RozengurtEnri... | lld:pubmed |
| pubmed-article:11948398 | pubmed:author | pubmed-author:HurdCliffC | lld:pubmed |
| pubmed-article:11948398 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11948398 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:11948398 | pubmed:volume | 21 | lld:pubmed |
| pubmed-article:11948398 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11948398 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11948398 | pubmed:pagination | 2154-60 | lld:pubmed |
| pubmed-article:11948398 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:11948398 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11948398 | pubmed:articleTitle | Protein kinase D complexes with C-Jun N-terminal kinase via activation loop phosphorylation and phosphorylates the C-Jun N-terminus. | lld:pubmed |
| pubmed-article:11948398 | pubmed:affiliation | Unit of Signal Transduction and Gastrointestinal Cancer, Division of Digestive Diseases, Department of Medicine, School of Medicine and Molecular Biology Institute, University of California, Los Angeles, California, CA 90095-1786, USA. | lld:pubmed |
| pubmed-article:11948398 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11948398 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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