Linked Life Data

21844210

Source:http://linkedlifedata.com/resource/pubmed/id/21844210

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-8-23
pubmed:abstractText
Aurora B kinase is essential for successful cell division and regulates spindle assembly and kinetochore-microtubule interactions. The kinase localizes to the inner centromere until anaphase, but many of its substrates have distinct localizations, for example on chromosome arms and at kinetochores. Furthermore, substrate phosphorylation depends on distance from the kinase. How the kinase reaches substrates at a distance and how spatial phosphorylation patterns are determined are unknown. In this paper, we show that a phosphorylation gradient is produced by Aurora B concentration and activation at centromeres and release and diffusion to reach substrates at a distance. Kinase concentration, either at centromeres or at another chromosomal site, is necessary for activity globally. By experimentally manipulating dynamic exchange at centromeres, we demonstrate that the kinase reaches its substrates by diffusion. We also directly observe, using a fluorescence resonance energy transfer-based biosensor, phosphorylation spreading from centromeres after kinase activation. We propose that Aurora B dynamics and diffusion from the inner centromere create spatial information to regulate cell division.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1540-8140
pubmed:author
pubmed:issnType
Electronic
pubmed:day
22
pubmed:volume
194
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
539-49
pubmed:meshHeading
pubmed-meshheading:21844210-Biosensing Techniques, pubmed-meshheading:21844210-Cell Cycle Proteins, pubmed-meshheading:21844210-Centromere, pubmed-meshheading:21844210-Chromosomal Proteins, Non-Histone, pubmed-meshheading:21844210-Diffusion, pubmed-meshheading:21844210-Enzyme Activation, pubmed-meshheading:21844210-Fluorescence Resonance Energy Transfer, pubmed-meshheading:21844210-HeLa Cells, pubmed-meshheading:21844210-Humans, pubmed-meshheading:21844210-Microscopy, Confocal, pubmed-meshheading:21844210-Microscopy, Video, pubmed-meshheading:21844210-Phosphorylation, pubmed-meshheading:21844210-Protein-Serine-Threonine Kinases, pubmed-meshheading:21844210-RNA Interference, pubmed-meshheading:21844210-Recombinant Fusion Proteins, pubmed-meshheading:21844210-Time Factors, pubmed-meshheading:21844210-Transfection
pubmed:year
2011
pubmed:articleTitle
Aurora B dynamics at centromeres create a diffusion-based phosphorylation gradient.
pubmed:affiliation
Department of Biology, University of Pennsylvania, Philadelphia, PA 19104, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural, Video-Audio Media