Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2008-9-5
pubmed:abstractText
The Arabidopsis (Arabidopsis thaliana) SOMATIC EMBRYOGENESIS RECEPTOR KINASE (SERK) genes belong to a small family of five plant receptor kinases that are involved in at least five different signaling pathways. One member of this family, BRASSINOSTEROID INSENSITIVE1 (BRI1)-ASSOCIATED KINASE1 (BAK1), also known as SERK3, is the coreceptor of the brassinolide (BR)-perceiving receptor BRI1, a function that is BR dependent and partially redundant with SERK1. BAK1 (SERK3) alone controls plant innate immunity, is also the coreceptor of the flagellin receptor FLS2, and, together with SERK4, can mediate cell death control, all three in a BR-independent fashion. SERK1 and SERK2 are essential for male microsporogenesis, again independent from BR. SERK5 does not appear to have any function under the conditions tested. Here, we show that the different SERK members are only redundant in pairs, whereas higher order mutant combinations only show additive phenotypes. Surprisingly, SERK members that are redundant within one are not redundant in another pathway. We also show that this evolution of functional pairs occurred by a change in protein function and not by differences in spatial expression. We propose that, in plants, closely related receptor kinases have a minimal homo- or heterodimeric configuration to achieve specificity.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-10069079, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-11130711, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-11320207, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-11526204, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-11706164, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-12007405, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-12150928, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-12150929, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-12154130, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-12401166, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-12724536, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-12724544, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-12893945, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-14615601, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-14617092, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-15548744, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-15894717, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-15908602, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-16284305, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-16284306, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-16829981, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-17163906, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-17583510, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-17600708, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-17626179, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-17905839, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-2554318, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-9169851, http://linkedlifedata.com/resource/pubmed/commentcorrection/18667726-9426607
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0032-0889
pubmed:author
pubmed:issnType
Print
pubmed:volume
148
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
611-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Arabidopsis SOMATIC EMBRYOGENESIS RECEPTOR KINASE proteins serve brassinosteroid-dependent and -independent signaling pathways.
pubmed:affiliation
Laboratory of Biochemistry, Wageningen University, 6703 HA Wageningen, The Netherlands. catherine.albrecht@wur.nl
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't