| pubmed-article:19711352 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19711352 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:19711352 | lifeskim:mentions | umls-concept:C0013352 | lld:lifeskim |
| pubmed-article:19711352 | lifeskim:mentions | umls-concept:C0040690 | lld:lifeskim |
| pubmed-article:19711352 | lifeskim:mentions | umls-concept:C0023693 | lld:lifeskim |
| pubmed-article:19711352 | lifeskim:mentions | umls-concept:C0919432 | lld:lifeskim |
| pubmed-article:19711352 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:19711352 | lifeskim:mentions | umls-concept:C1524075 | lld:lifeskim |
| pubmed-article:19711352 | lifeskim:mentions | umls-concept:C1514873 | lld:lifeskim |
| pubmed-article:19711352 | lifeskim:mentions | umls-concept:C0337112 | lld:lifeskim |
| pubmed-article:19711352 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:19711352 | pubmed:dateCreated | 2009-10-1 | lld:pubmed |
| pubmed-article:19711352 | pubmed:abstractText | We have previously reported that the dynein light chain (DLC) km23-1 is required for Smad2-dependent TGFbeta signaling. Here we describe another member of the km23/DYNLRB/LC7/robl family of DLCs, termed km23-2, which is also involved in TGFbeta signaling. We show not only that TGFbeta stimulates the interaction of km23-2 (DYNLRB2) with TGFbeta receptor II (TbetaRII) but also that TGFbeta regulates the interaction between km23-2 and endogenous TbetaRII in vivo. In addition, TGFbeta treatment causes km23-2 phosphorylation, whereas a kinase-deficient form of TbetaRII prevents km23-2 phosphorylation. In contrast to the km23-1 isoform, blockade of km23-2 expression using small interfering RNAs (siRNAs) decreased key TGFbeta/Smad3-specific responses, including the induction of both plasminogen activator inhibitor-1 (PAI-1) gene expression and p21 protein expression. Blockade of km23-1 expression had no effect on these two major TGFbeta/Smad3 responses under similar conditions. Further, km23-2 was required for TGFbeta stimulation of Smad3-dependent Smad-binding element (SBE)2-Luc transcriptional activity, but not for TGFbeta stimulation of Smad2-dependent activin responsive element (ARE)-Lux transcriptional activity. In order to assess the mechanisms underlying the preferential stimulation of Smad3- versus Smad2-specific TGFbeta responses, immunoprecipitation (IP)/blot analyses were performed, which demonstrate that TGFbeta stimulated preferential complex formation of km23-2 with Smad3, relative to Smad2. Collectively, our findings indicate that km23-2 is required for Smad3-dependent TGFbeta signaling. More importantly, we demonstrate that km23-2 has functions in TGFbeta signaling that are distinct from those for km23-1. This is the first report to describe a differential requirement for unique isoforms of a specific DLC family in Smad-specific TGFbeta signaling. | lld:pubmed |
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| pubmed-article:19711352 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:19711352 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19711352 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19711352 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:19711352 | pubmed:issn | 1097-4652 | lld:pubmed |
