Linked Life Data

18235218

Source:http://linkedlifedata.com/resource/pubmed/id/18235218

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-4-21
pubmed:abstractText
Inhibition of the protein phosphatase 2A (PP2A) family of serine-threonine phosphatases contributes to human cell transformation. Depletion of PP2A complexes containing the PP2A B56gamma regulatory subunit in immortalized human cells induces cell transformation in vitro. To examine the function of PP2A B56gamma complexes, we applied tandem affinity purification and mass spectrometry to detect proteins that bind to PP2A B56gamma. We identified liprin alpha1 as a novel PP2A B56gamma interacting protein. B56gamma-liprin alpha1 complexes are distinct from PP2A complexes containing B56gamma. Consistent with this finding, liprin alpha1 does not directly contribute to cell transformation. However, suppression of liprin alpha1 by RNA interference alters cell morphology. These findings suggest a novel role for PP2A B56gamma independent of its regulation of PP2A activity.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
1551-4005
pubmed:author
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
525-32
pubmed:dateRevised
2008-9-23
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Liprin alpha1 interacts with PP2A B56gamma.
pubmed:affiliation
Department of Medical Oncology, Dana-Farber Cancer Institute, 44 Binney Street, Dana 1538, Boston, Massachusetts 02115, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural