Linked Life Data

20067996

Source:http://linkedlifedata.com/resource/pubmed/id/20067996

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 3
pubmed:dateCreated
2010-2-4
pubmed:abstractText
End-binding 1 (EB1) proteins are evolutionarily conserved plus-end-tracking proteins that localize to growing microtubule plus ends where they regulate microtubule dynamics and interactions with intracellular targets. Animal EB1 proteins have acidic C-terminal tails that might induce an autoinhibitory conformation. Although EB1 proteins with the same structural features occur in plants (EB1a and EB1b in Arabidopsis thaliana), a variant form (EB1c) is present that lacks the characteristic tail. We show that in Arabidopsis the tail region of EB1b, but not of EB1c, inhibits microtubule assembly in vitro. EB1a and EB1b form heterodimers with each other, but not with EB1c. Furthermore, the EB1 genes are expressed in various cell types of Arabidopsis, but the expression of EB1c is particularly strong in the meristematic cells where it is targeted to the nucleus by a nuclear localization signal in the C-terminal tail. Reduced expression of EB1c compromised the alignment of spindle and phragmoplast microtubules and caused frequent lagging of separating chromosomes at anaphase. Roots of the eb1c mutant were hypersensitive to a microtubule-disrupting drug and complete rescue of the mutant phenotype required the tail region of EB1c. These results suggest that a plant-specific EB1 subtype has evolved to function preferentially on the spindle microtubules by accumulating in the prophase nucleus.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1477-9137
pubmed:author
pubmed:issnType
Electronic
pubmed:day
1
pubmed:volume
123
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
451-9
pubmed:meshHeading
pubmed-meshheading:20067996-Amino Acid Sequence, pubmed-meshheading:20067996-Arabidopsis, pubmed-meshheading:20067996-Arabidopsis Proteins, pubmed-meshheading:20067996-Cell Nucleus, pubmed-meshheading:20067996-Chromosome Segregation, pubmed-meshheading:20067996-Dinitrobenzenes, pubmed-meshheading:20067996-Microtubules, pubmed-meshheading:20067996-Mitotic Spindle Apparatus, pubmed-meshheading:20067996-Molecular Sequence Data, pubmed-meshheading:20067996-Phenotype, pubmed-meshheading:20067996-Plant Roots, pubmed-meshheading:20067996-Plants, Genetically Modified, pubmed-meshheading:20067996-Protein Multimerization, pubmed-meshheading:20067996-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:20067996-Sequence Homology, Amino Acid, pubmed-meshheading:20067996-Sulfanilamides, pubmed-meshheading:20067996-Tobacco
pubmed:year
2010
pubmed:articleTitle
Nuclear-localized subtype of end-binding 1 protein regulates spindle organization in Arabidopsis.
pubmed:affiliation
Graduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't