Linked Life Data

10413518

Source:http://linkedlifedata.com/resource/pubmed/id/10413518

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
29
pubmed:dateCreated
1999-9-15
pubmed:abstractText
Lamina-associated polypeptide 2 beta (LAP 2 beta), an integral protein of the inner nuclear membrane, appears to be involved in the spatial organization of the interface between nucleoplasma, lamina, and nuclear envelope. Its ability to interact with other proteins and the structural integrity of the nuclear envelope is probably regulated by phosphorylation. Here, we report nonmitotic LAP 2 beta phosphorylation sites that are phosphorylated in the native protein when purified from nuclear envelopes of mouse neuroblastoma Neuro2a cells. Five phosphorylation sites were detected by nano-electrospray mass spectrometric analysis of tryptic LAP 2 beta peptides using parent ion scans specific for phosphopeptides. By mass spectrometric sequencing of these peptides, we identified as phosphorylated residues Thr 74, Thr 159, Ser 176, and Ser 179. Two of the phosphorylation sites, Thr 74 (within a region known to bind chromatin) and Thr 159, are part of consensus sequences of proline-directed kinases. Ser 179 is part of a consensus site for protein kinase C which is able to highly phosphorylate LAP 2 beta in vitro. Three phosphorylation sites, Thr 159, Ser 176, and Ser 179, are located within a stretch of 20 amino acids, thereby forming a highly phosphorylated protein domain which may integrate signaling by multiple protein kinases. Additionally, we identified for the first time at the protein level the LAP 2 splice variant LAP 2 epsilon in nuclear envelopes.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9426-34
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:10413518-Amino Acid Sequence, pubmed-meshheading:10413518-Animals, pubmed-meshheading:10413518-DNA-Binding Proteins, pubmed-meshheading:10413518-Membrane Proteins, pubmed-meshheading:10413518-Mice, pubmed-meshheading:10413518-Molecular Sequence Data, pubmed-meshheading:10413518-Neoplasm Proteins, pubmed-meshheading:10413518-Neuroblastoma, pubmed-meshheading:10413518-Nuclear Envelope, pubmed-meshheading:10413518-Nuclear Proteins, pubmed-meshheading:10413518-Phosphopeptides, pubmed-meshheading:10413518-Phosphorylation, pubmed-meshheading:10413518-Protein Kinase C, pubmed-meshheading:10413518-Protein-Serine-Threonine Kinases, pubmed-meshheading:10413518-Protein-Tyrosine Kinases, pubmed-meshheading:10413518-Substrate Specificity, pubmed-meshheading:10413518-Tumor Cells, Cultured
pubmed:year
1999
pubmed:articleTitle
Identification of phosphorylation sites in native lamina-associated polypeptide 2 beta.
pubmed:affiliation
AG Neurochemie, Institut für Biochemie, Freie Universität Berlin, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't