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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5609
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pubmed:dateCreated |
2003-2-14
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pubmed:abstractText |
How scaffold proteins control information flow in signaling pathways is poorly understood: Do they simply tether components, or do they precisely orient and activate them? We found that the yeast mitogen-activated protein (MAP) kinase scaffold Ste5 is tolerant to major stereochemical perturbations; heterologous protein interactions could functionally replace native kinase recruitment interactions, indicating that simple tethering is largely sufficient for scaffold-mediated signaling. Moreover, by engineering a scaffold that tethers a unique kinase set, we could create a synthetic MAP kinase pathway with non-natural input-output properties. These findings demonstrate that scaffolds are highly flexible organizing factors that can facilitate pathway evolution and engineering.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/FUS3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/HOG1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/MF alpha protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinase...,
http://linkedlifedata.com/resource/pubmed/chemical/Mitogen-Activated Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/PBS2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SHO1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/STE11 protein kinase,
http://linkedlifedata.com/resource/pubmed/chemical/STE5 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/STE7 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
14
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pubmed:volume |
299
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1061-4
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12511654-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:12511654-Binding Sites,
pubmed-meshheading:12511654-Carrier Proteins,
pubmed-meshheading:12511654-Evolution, Molecular,
pubmed-meshheading:12511654-MAP Kinase Kinase Kinases,
pubmed-meshheading:12511654-MAP Kinase Signaling System,
pubmed-meshheading:12511654-Membrane Proteins,
pubmed-meshheading:12511654-Mitogen-Activated Protein Kinase Kinases,
pubmed-meshheading:12511654-Mitogen-Activated Protein Kinases,
pubmed-meshheading:12511654-Mutation,
pubmed-meshheading:12511654-Osmolar Concentration,
pubmed-meshheading:12511654-Phosphorylation,
pubmed-meshheading:12511654-Protein Binding,
pubmed-meshheading:12511654-Protein Conformation,
pubmed-meshheading:12511654-Protein Kinases,
pubmed-meshheading:12511654-Protein Precursors,
pubmed-meshheading:12511654-Protein Structure, Tertiary,
pubmed-meshheading:12511654-Recombinant Fusion Proteins,
pubmed-meshheading:12511654-Saccharomyces cerevisiae,
pubmed-meshheading:12511654-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:12511654-Substrate Specificity
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pubmed:year |
2003
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pubmed:articleTitle |
Rewiring MAP kinase pathways using alternative scaffold assembly mechanisms.
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pubmed:affiliation |
Department of Cellular and Molecular Pharmacology and Department of Biochemistry and Biophysics, University of California, 513 Parnassus Avenue, San Francisco, CA 94143, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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