Linked Life Data

1696578

Source:http://linkedlifedata.com/resource/pubmed/id/1696578

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1990-9-20
pubmed:abstractText
At the onset of mitosis a class of proteins appears that possess a phosphorylated epitope recognized by the monoclonal antibody MPM-2. Immunofluorescence staining shows that a subset of these proteins is associated with the centrosomes of the mitotic apparatus. The appearance of these proteins coincides with the increased microtubule nucleating capacity of the centrosomes. We have tested whether growth of microtubules from mitotic centrosomes in a lysed cell model is dependent on the availability of the phosphorylated epitope by blocking the epitope with a specific antibody or by modifying it by removal of the phosphate. Centrosomes incubated with purified tubulin nucleate microtubule asters. However, preincubating the centrosomes with MPM-2 blocks all microtubule nucleation. Pretreating mitotic centrosomes with alkaline phosphatase also inhibits nucleation. These data suggest that the phosphorylated epitope recognized by MPM-2 is important for microtubule nucleation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
95 ( Pt 3)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
405-11
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Nucleation of microtubules from mitotic centrosomes is modulated by a phosphorylated epitope.
pubmed:affiliation
Laboratory of Molecular Biology, University of Wisconsin-Madison 53706.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.