Linked Life Data

7961788

Source:http://linkedlifedata.com/resource/pubmed/id/7961788

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
45
pubmed:dateCreated
1994-12-16
pubmed:abstractText
The receptor-type protein tyrosine phosphatase PTP mu comprises an extracellular segment containing a MAM domain, an immunoglobulin domain and four fibronectin type III repeats, a transmembrane segment, and two intracellular PTP domains. We have previously shown that PTP mu binds homophilically, i.e. PTP mu on the surface of one cell binds to PTP mu on an apposing cell, and that the extracellular segment alone is sufficient for homophilic binding. In this study we report that in MvLu cells PTP mu is proteolytically processed into two noncovalently associated fragments, one comprising most of the extracellular segment (approximately 100 kDa) and the other containing predominantly the transmembrane and intracellular portions (approximately 100 kDa). We have also identified the homophilic binding site within the extracellular segment. We have generated, expressed, and purified various fragments of the extracellular segment of PTP mu and have used fluorescent beads (Covaspheres) coated with these fragments in three binding assays: (i) measurement of bead aggregation, (ii) binding of beads to surfaces of dishes coated with purified PTP mu, or (iii) binding to MvLu cells. Only beads coated with recombinant fragments that contained the immunoglobulin domain underwent aggregation or bound to surfaces displaying PTP mu, suggesting that neither the MAM domain nor the fibronectin type III repeats bound homophilically in these assays. The fragment containing the Ig domain alone bound as well as any other Ig domain-containing fragment, suggesting that the Ig domain is both necessary and sufficient for homophilic binding under these conditions.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
269
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
28472-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:7961788-Animals, pubmed-meshheading:7961788-Antibodies, Monoclonal, pubmed-meshheading:7961788-Binding Sites, pubmed-meshheading:7961788-Cell Line, pubmed-meshheading:7961788-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:7961788-Humans, pubmed-meshheading:7961788-Immunoblotting, pubmed-meshheading:7961788-Macromolecular Substances, pubmed-meshheading:7961788-Membrane Proteins, pubmed-meshheading:7961788-Peptide Fragments, pubmed-meshheading:7961788-Polymerase Chain Reaction, pubmed-meshheading:7961788-Protein Processing, Post-Translational, pubmed-meshheading:7961788-Protein Tyrosine Phosphatases, pubmed-meshheading:7961788-Receptor-Like Protein Tyrosine Phosphatases, Class 2, pubmed-meshheading:7961788-Receptor-Like Protein Tyrosine Phosphatases, Class 8, pubmed-meshheading:7961788-Spodoptera, pubmed-meshheading:7961788-Transfection
pubmed:year
1994
pubmed:articleTitle
Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTP mu.
pubmed:affiliation
Cold Spring Harbor Laboratory, New York 11724-2208.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't