| pubmed-article:19827767 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19827767 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:19827767 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:19827767 | lifeskim:mentions | umls-concept:C0031727 | lld:lifeskim |
| pubmed-article:19827767 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:19827767 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:19827767 | pubmed:issue | 46 | lld:pubmed |
| pubmed-article:19827767 | pubmed:dateCreated | 2009-11-17 | lld:pubmed |
| pubmed-article:19827767 | pubmed:abstractText | Src family kinases (SFKs) are modular signaling proteins possessing SH3, SH2, and tyrosine kinase domains. The SH3 and SH2 domains of SFKs have dual roles: they regulate the activity of the kinases, and they also target SFKs to their cellular substrates. We generated a series of novel SFKs by replacing the SH2 and SH3 domains of Hck with the syntrophin PDZ domain. In some constructs, the negative regulatory tyrosine in the C-terminal tail was also replaced with a PDZ ligand sequence. When expressed in mammalian cells, the substrate specificity of the PDZ-kinases was directed to a different group of proteins than wild-type Hck. The PDZ-kinases phosphorylate neuronal nitric oxide synthase (nNOS), a known binding partner of the syntrophin PDZ domain. We also introduced a PDZ ligand at the C-terminus of the adaptor protein Cas. PDZ-Hck kinases phosphorylate the engineered Cas protein in Cas(-/-) cells and restore the migration defect of these cells. A PDZ-kinase was also functional in rewiring MAPK signaling via an engineered ErbB2 construct containing a PDZ ligand sequence. Several of the PDZ-kinases show autoregulatory properties similar to natural SFKs. Thus, the PDZ-ligand interaction is able to functionally replace the normal SH2-pY527 interaction that regulates SFKs. Our data highlight the modularity and evolvability of signaling proteins. | lld:pubmed |
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| pubmed-article:19827767 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19827767 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19827767 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19827767 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:19827767 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19827767 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:19827767 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:19827767 | pubmed:author | pubmed-author:MillerW... | lld:pubmed |
| pubmed-article:19827767 | pubmed:author | pubmed-author:LimWendell... | lld:pubmed |
| pubmed-article:19827767 | pubmed:author | pubmed-author:YehBrian JBJ | lld:pubmed |
| pubmed-article:19827767 | pubmed:author | pubmed-author:CraddockBarba... | lld:pubmed |
| pubmed-article:19827767 | pubmed:author | pubmed-author:YadavShalini... | lld:pubmed |
| pubmed-article:19827767 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19827767 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:19827767 | pubmed:volume | 48 | lld:pubmed |
| pubmed-article:19827767 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19827767 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19827767 | pubmed:pagination | 10956-62 | lld:pubmed |
| pubmed-article:19827767 | pubmed:dateRevised | 2010-12-28 | lld:pubmed |
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