Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5479
pubmed:dateCreated
2000-8-8
pubmed:abstractText
The CLAVATA1 (CLV1) and CLAVATA3 (CLV3) proteins form a potential receptor and ligand pair that regulates the balance between cell proliferation and differentiation at the shoot meristem of Arabidopsis. CLV1 encodes a receptor-kinase, and CLV3 encodes a predicted small, secreted polypeptide. We demonstrate that the CLV3 and CLV1 proteins coimmunoprecipitate in vivo, that yeast cells expressing CLV1 and CLV2 bind to CLV3 from plant extracts, and that binding requires CLV1 kinase activity. CLV3 only associates with the presumed active CLV1 protein complex in vivo. More than 75% of CLV3 in cauliflower extracts is bound with CLV1, consistent with hypotheses of ligand sequestration. Soluble CLV3 was found in an approximately 25-kilodalton multimeric complex.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers, http://linkedlifedata.com/resource/pubmed/chemical/CLV1 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/CLV2 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/CLV3 protein, Arabidopsis, http://linkedlifedata.com/resource/pubmed/chemical/Immune Sera, http://linkedlifedata.com/resource/pubmed/chemical/Ligands, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Plant Extracts, http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptor Protein-Tyrosine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0036-8075
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
289
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
613-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10915623-Alleles, pubmed-meshheading:10915623-Arabidopsis, pubmed-meshheading:10915623-Arabidopsis Proteins, pubmed-meshheading:10915623-Biopolymers, pubmed-meshheading:10915623-Brassica, pubmed-meshheading:10915623-Cell Membrane, pubmed-meshheading:10915623-Genes, Plant, pubmed-meshheading:10915623-Immune Sera, pubmed-meshheading:10915623-Ligands, pubmed-meshheading:10915623-Membrane Proteins, pubmed-meshheading:10915623-Meristem, pubmed-meshheading:10915623-Molecular Weight, pubmed-meshheading:10915623-Plant Extracts, pubmed-meshheading:10915623-Plant Proteins, pubmed-meshheading:10915623-Protein Binding, pubmed-meshheading:10915623-Receptor Protein-Tyrosine Kinases, pubmed-meshheading:10915623-Recombinant Fusion Proteins, pubmed-meshheading:10915623-Signal Transduction
pubmed:year
2000
pubmed:articleTitle
CLAVATA3, a multimeric ligand for the CLAVATA1 receptor-kinase.
pubmed:affiliation
Department of Biology, University of Michigan, Ann Arbor, MI 48109-1048, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Retracted Publication