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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 |
2011-2-3
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pubmed:abstractText |
Receptor tyrosine kinases control many critical processes in metazoans, but these enzymes appear to be absent in plants. Recently, two Arabidopsis receptor kinases--BRASSINOSTEROID INSENSITIVE 1 (BRI1) and BRI1-ASSOCIATED KINASE1 (BAK1), the receptor and coreceptor for brassinosteroids--were shown to autophosphorylate on tyrosines. However, the cellular roles for tyrosine phosphorylation in plants remain poorly understood. Here, we report that the BRI1 KINASE INHIBITOR 1 (BKI1) is tyrosine phosphorylated in response to brassinosteroid perception. Phosphorylation occurs within a reiterated [KR][KR] membrane targeting motif, releasing BKI1 into the cytosol and enabling formation of an active signaling complex. Our work reveals that tyrosine phosphorylation is a conserved mechanism controlling protein localization in all higher organisms.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-11027724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-11526204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-11678275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-11891123,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-12471243,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-14580337,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-17889650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-18046415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-18508681,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-19124768,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-19282669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-19734888,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/21289069-20876109
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1549-5477
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
232-7
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pubmed:dateRevised |
2011-8-3
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pubmed:meshHeading |
pubmed-meshheading:21289069-Amino Acid Motifs,
pubmed-meshheading:21289069-Amino Acid Sequence,
pubmed-meshheading:21289069-Arabidopsis,
pubmed-meshheading:21289069-Arabidopsis Proteins,
pubmed-meshheading:21289069-Cell Membrane,
pubmed-meshheading:21289069-Conserved Sequence,
pubmed-meshheading:21289069-Enzyme Activation,
pubmed-meshheading:21289069-Models, Molecular,
pubmed-meshheading:21289069-Mutation,
pubmed-meshheading:21289069-Phosphorylation,
pubmed-meshheading:21289069-Protein Binding,
pubmed-meshheading:21289069-Protein Kinases,
pubmed-meshheading:21289069-Protein Structure, Tertiary,
pubmed-meshheading:21289069-Protein Transport,
pubmed-meshheading:21289069-Protein-Serine-Threonine Kinases,
pubmed-meshheading:21289069-Sequence Alignment,
pubmed-meshheading:21289069-Tyrosine
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pubmed:year |
2011
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pubmed:articleTitle |
Tyrosine phosphorylation controls brassinosteroid receptor activation by triggering membrane release of its kinase inhibitor.
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pubmed:affiliation |
Plant Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, CA 92037, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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