| pubmed-article:14743217 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14743217 | lifeskim:mentions | umls-concept:C0025252 | lld:lifeskim |
| pubmed-article:14743217 | lifeskim:mentions | umls-concept:C0596156 | lld:lifeskim |
| pubmed-article:14743217 | lifeskim:mentions | umls-concept:C0887838 | lld:lifeskim |
| pubmed-article:14743217 | lifeskim:mentions | umls-concept:C0258823 | lld:lifeskim |
| pubmed-article:14743217 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:14743217 | lifeskim:mentions | umls-concept:C0337094 | lld:lifeskim |
| pubmed-article:14743217 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:14743217 | pubmed:dateCreated | 2004-2-2 | lld:pubmed |
| pubmed-article:14743217 | pubmed:abstractText | Protein kinase D (PKD) binds to diacylglycerol (DAG) in the trans-Golgi network (TGN) and is activated by trimeric G-protein subunits beta gamma. This complex then regulates the formation of transport carriers in the TGN that traffic to the plasma membrane in non-polarized cells. Here we report specificity of different PKD isoforms in regulating protein trafficking from the TGN. Kinase-inactive forms of PKD1, PKD2 and PKD3 localize to the TGN in polarized and non-polarized cells. PKD activity is required only for the transport of proteins containing basolateral sorting information, and seems to be cargo specific. | lld:pubmed |
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| pubmed-article:14743217 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14743217 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14743217 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14743217 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14743217 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14743217 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14743217 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:14743217 | pubmed:issn | 1465-7392 | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:MalhotraVivek... | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:YeamanCharles... | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:NelsonW... | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:MellmanIraI | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:SeufferleinTh... | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:BardFredericF | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:MaedaYusukeY | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:BossardCarine... | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:BINETJ PJP | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:AyalaM... | lld:pubmed |
| pubmed-article:14743217 | pubmed:author | pubmed-author:WrightJessica... | lld:pubmed |
| pubmed-article:14743217 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14743217 | pubmed:volume | 6 | lld:pubmed |
| pubmed-article:14743217 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14743217 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14743217 | pubmed:pagination | 106-12 | lld:pubmed |
| pubmed-article:14743217 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:14743217 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14743217 | pubmed:articleTitle | Protein kinase D regulates basolateral membrane protein exit from trans-Golgi network. | lld:pubmed |
| pubmed-article:14743217 | pubmed:affiliation | Department of Anatomy and Cell Biology, University of Iowa, Iowa City, IA 52242-1109, USA. | lld:pubmed |
| pubmed-article:14743217 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14743217 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14743217 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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