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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2005-6-3
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pubmed:abstractText |
Leucine-rich repeat (LRR)-containing transmembrane receptor-like kinases (RLKs) are important components of plant signal transduction. The Arabidopsis thaliana somatic embryogenesis receptor-like kinase 1 (AtSERK1) is an LRR-RLK proposed to participate in a signal transduction cascade involved in embryo development. By yeast two-hybrid screening we identified AtCDC48, a homologue of the mammalian AAA-ATPase p97 and GF14lambda, a member of the Arabidopsis family of 14-3-3 proteins as AtSERK1 interactors. In vitro, the AtSERK1 kinase domain is able to transphosphorylate and bind both AtCDC48 and GF14lambda. In yeast, AtCDC48 interacts with GF14lambda and with the PP2C phosphatase KAPP. In plant protoplasts AtSERK1 interacts with GF14lambda.
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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/14-3-3 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/AFT1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/CDC48 protein,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/KAPP protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SERK1 protein, Arabidopsis,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/protein phosphatase 2C
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0032-0935
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
221
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
394-405
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15592873-14-3-3 Proteins,
pubmed-meshheading:15592873-Adenosine Triphosphatases,
pubmed-meshheading:15592873-Arabidopsis,
pubmed-meshheading:15592873-Arabidopsis Proteins,
pubmed-meshheading:15592873-Binding Sites,
pubmed-meshheading:15592873-Cell Cycle Proteins,
pubmed-meshheading:15592873-Gene Expression Profiling,
pubmed-meshheading:15592873-Phosphoprotein Phosphatases,
pubmed-meshheading:15592873-Phosphorylation,
pubmed-meshheading:15592873-Protein Binding,
pubmed-meshheading:15592873-Protein Kinases,
pubmed-meshheading:15592873-Protoplasts,
pubmed-meshheading:15592873-Recombinant Fusion Proteins,
pubmed-meshheading:15592873-Signal Transduction,
pubmed-meshheading:15592873-Trans-Activators,
pubmed-meshheading:15592873-Two-Hybrid System Techniques
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pubmed:year |
2005
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pubmed:articleTitle |
The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP.
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pubmed:affiliation |
Laboratory of Biochemistry, Department of Agrotechnology and Food Sciences, Wageningen University and Research Centre, Dreijenlaan 3, 6703, HA, Wageningen, The Netherlands.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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