Linked Life Data

16105548

Source:http://linkedlifedata.com/resource/pubmed/id/16105548

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2005-8-17
pubmed:abstractText
Pleiotrophin (PTN the protein, Ptn the gene) signals through a unique mechanism; it inactivates the tyrosine phosphatase activity of its receptor, the transmembrane receptor protein tyrosine phosphatase (RPTP)beta/zeta, and increases tyrosine phosphorylation of the substrates of RPTPbeta/zeta through the continued activity of a yet to be described protein tyrosine kinase(s) in PTN-stimulated cells. We have now found that the cytoskeletal protein beta-adducin interacts with the intracellular domain of RPTPbeta/zeta in a yeast two-hybrid system, that beta-adducin is a substrate of RPTPbeta/zeta, that beta-adducin is phosphorylated in tyrosine in cells not stimulated by PTN, and that tyrosine phosphorylation of beta-adducin is sharply increased in PTN-stimulated cells, suggesting that beta-adducin is a downstream target of and regulated by the PTN/RPTPbeta/zeta signaling pathway. beta-Catenin was the first downstream target of the PTN/RPTPbeta/zeta signaling pathway to be identified; these data thus also suggest that PTN coordinately regulates steady state levels of tyrosine phosphorylation of the important cytoskeletal proteins beta-adducin and beta-catenin and, through PTN-stimulated tyrosine phosphorylation, beta-adducin may contribute to the disruption of cytoskeletal structure, increased plasticity, and loss of homophilic cell-cell adhesion that are the consequences of PTN stimulation of cells and a characteristic feature of different malignant cells with mutations that activate constitutive expression of the endogenous Ptn gene.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
335
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
232-9
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:16105548-Amino Acid Sequence, pubmed-meshheading:16105548-Animals, pubmed-meshheading:16105548-Binding Sites, pubmed-meshheading:16105548-Calmodulin-Binding Proteins, pubmed-meshheading:16105548-Carrier Proteins, pubmed-meshheading:16105548-Cell Line, pubmed-meshheading:16105548-Cytokines, pubmed-meshheading:16105548-Enzyme Activation, pubmed-meshheading:16105548-Humans, pubmed-meshheading:16105548-Molecular Sequence Data, pubmed-meshheading:16105548-Nerve Tissue Proteins, pubmed-meshheading:16105548-Peptide Fragments, pubmed-meshheading:16105548-Phosphorylation, pubmed-meshheading:16105548-Phosphotyrosine, pubmed-meshheading:16105548-Protein Binding, pubmed-meshheading:16105548-Protein Tyrosine Phosphatases, pubmed-meshheading:16105548-Receptor-Like Protein Tyrosine Phosphatases, Class 5, pubmed-meshheading:16105548-Saccharomyces cerevisiae, pubmed-meshheading:16105548-Sequence Alignment, pubmed-meshheading:16105548-Substrate Specificity, pubmed-meshheading:16105548-Two-Hybrid System Techniques
pubmed:year
2005
pubmed:articleTitle
Pleiotrophin stimulates tyrosine phosphorylation of beta-adducin through inactivation of the transmembrane receptor protein tyrosine phosphatase beta/zeta.
pubmed:affiliation
Department of Molecular and Experimental Medicine, Department of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural