| pubmed-article:15980428 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15980428 | lifeskim:mentions | umls-concept:C0019360 | lld:lifeskim |
| pubmed-article:15980428 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:15980428 | lifeskim:mentions | umls-concept:C0007586 | lld:lifeskim |
| pubmed-article:15980428 | lifeskim:mentions | umls-concept:C0110613 | lld:lifeskim |
| pubmed-article:15980428 | pubmed:issue | 34 | lld:pubmed |
| pubmed-article:15980428 | pubmed:dateCreated | 2005-8-22 | lld:pubmed |
| pubmed-article:15980428 | pubmed:abstractText | Gap junction channels play an important role in cell growth control, secretion and embryonic development. Gap junctional communication and channel assembly can be regulated by protein-protein interaction with kinases and phosphatases. We have utilized tandem mass spectrometry (MS/MS) sequence analysis as a screen to identify proteins from cell lysates that interact with the C-terminal cytoplasmic region of connexin 43 (Cx43). MS/MS analysis of tryptic fragments yielded several proteins including zona occludens-1 (ZO-1), a structural protein previously identified to interact with Cx43, and ZO-2, a potential novel interacting partner. We confirmed the interaction of ZO-2 with Cx43 by using a combination of fusion protein "pull down," co-immunoprecipitation, and co-localization experiments. We show that the C-terminal region of Cx43 is necessary for interaction with the PDZ2 domain of ZO-2. Far Western analysis revealed that ZO-2 can directly bind to Cx43 independent of other interacting partners. Immunofluorescence studies indicate that both ZO-1 and ZO-2 can co-localize with Cx43 within the plasma membrane at apparent gap junctional structures. We examined Cx43 interaction with ZO-1 and ZO-2 at different stages of the cell cycle and found that Cx43 had a strong preference for interaction with ZO-1 during G0, whereas ZO-2 interaction occurred approximately equally during G0 and S phases. Since essentially all of the Cx43 in G0 cells is assembled into Triton X-100-resistant junctions, Cx43-ZO-1 interaction may contribute to their stability. | lld:pubmed |
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| pubmed-article:15980428 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15980428 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15980428 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15980428 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:15980428 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15980428 | pubmed:author | pubmed-author:TaffetSteven... | lld:pubmed |
| pubmed-article:15980428 | pubmed:author | pubmed-author:LampePaul DPD | lld:pubmed |
| pubmed-article:15980428 | pubmed:author | pubmed-author:SolanJoell... | lld:pubmed |
| pubmed-article:15980428 | pubmed:author | pubmed-author:SinghDeepikaD | lld:pubmed |
| pubmed-article:15980428 | pubmed:author | pubmed-author:JavierRonaldR | lld:pubmed |
| pubmed-article:15980428 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15980428 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:15980428 | pubmed:volume | 280 | lld:pubmed |
| pubmed-article:15980428 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15980428 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15980428 | pubmed:pagination | 30416-21 | lld:pubmed |
| pubmed-article:15980428 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:15980428 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:15980428 | pubmed:articleTitle | Connexin 43 interacts with zona occludens-1 and -2 proteins in a cell cycle stage-specific manner. | lld:pubmed |
| pubmed-article:15980428 | pubmed:affiliation | Division of Public Health Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA. | lld:pubmed |
| pubmed-article:15980428 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15980428 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15980428 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:15980428 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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