| pubmed-article:18431466 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18431466 | lifeskim:mentions | umls-concept:C0231239 | lld:lifeskim |
| pubmed-article:18431466 | lifeskim:mentions | umls-concept:C1523273 | lld:lifeskim |
| pubmed-article:18431466 | lifeskim:mentions | umls-concept:C1441672 | lld:lifeskim |
| pubmed-article:18431466 | lifeskim:mentions | umls-concept:C0037812 | lld:lifeskim |
| pubmed-article:18431466 | lifeskim:mentions | umls-concept:C0016315 | lld:lifeskim |
| pubmed-article:18431466 | lifeskim:mentions | umls-concept:C0279268 | lld:lifeskim |
| pubmed-article:18431466 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:18431466 | pubmed:dateCreated | 2008-4-23 | lld:pubmed |
| pubmed-article:18431466 | pubmed:abstractText | Sterile-alpha-motif (SAM) domains are common protein interaction motifs observed in organisms as diverse as yeast and human. They play a role in protein homo- and hetero-interactions in processes ranging from signal transduction to RNA binding. In addition, mutations in SAM domain and SAM-mediated oligomers have been linked to several diseases. To date, the observation of heterogeneous SAM-mediated oligomers in vivo has been elusive, which represents a common challenge in dissecting cellular biochemistry in live-cell systems. In this study, we report the oligomerization and binding stoichiometry of high-order, multi-component complexes of (SAM) domain proteins Ste11 and Ste50 in live yeast cells using fluorescence fluctuation methods. Fluorescence cross-correlation spectroscopy (FCCS) and 1-dimensional photon counting histogram (1dPCH) confirm the SAM-mediated interaction and oligomerization of Ste11 and Ste50. Two-dimensional PCH (2dPCH), with endogenously expressed proteins tagged with GFP or mCherry, uniquely indicates that Ste11 and Ste50 form a heterogeneous complex in the yeast cytosol comprised of a dimer of Ste11 and a monomer of Ste50. In addition, Ste50 also exists as a high order oligomer that does not interact with Ste11, and the size of this oligomer decreases in response to signals that activate the MAP kinase cascade. Surprisingly, a SAM domain mutant of Ste50 disrupted not only the Ste50 oligomers but also Ste11 dimerization. These results establish an in vivo model of Ste50 and Ste11 homo- and hetero-oligomerization and highlight the usefulness of 2dPCH for quantitative dissection of complex molecular interactions in genetic model organisms such as yeast. | lld:pubmed |
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| pubmed-article:18431466 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18431466 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18431466 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18431466 | pubmed:issn | 1932-6203 | lld:pubmed |
| pubmed-article:18431466 | pubmed:author | pubmed-author:TranJ VJV | lld:pubmed |
| pubmed-article:18431466 | pubmed:author | pubmed-author:SchwartzJoel... | lld:pubmed |
| pubmed-article:18431466 | pubmed:author | pubmed-author:SlaughterBria... | lld:pubmed |
| pubmed-article:18431466 | pubmed:author | pubmed-author:WiegraebeWinf... | lld:pubmed |
| pubmed-article:18431466 | pubmed:author | pubmed-author:HuffJoseph... | lld:pubmed |
| pubmed-article:18431466 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18431466 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:18431466 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18431466 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18431466 | pubmed:pagination | e1931 | lld:pubmed |
| pubmed-article:18431466 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:18431466 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18431466 | pubmed:articleTitle | SAM domain-based protein oligomerization observed by live-cell fluorescence fluctuation spectroscopy. | lld:pubmed |
| pubmed-article:18431466 | pubmed:affiliation | The Stowers Institute for Medical Research, Kansas City, Missouri, United States of America. | lld:pubmed |
| pubmed-article:18431466 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18431466 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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