Linked Life Data

7685348

Source:http://linkedlifedata.com/resource/pubmed/id/7685348

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
17
pubmed:dateCreated
1993-7-13
pubmed:abstractText
F1-20 and AP-3 are independently described, synapse-associated, developmentally regulated phosphoproteins with similar apparent molecular masses on SDS-polyacrylamide gel electrophoresis (PAGE). F1-20 was cloned and characterized because of its synapse specificity. AP-3 was purified and studied biochemically because of its function as a clathrin assembly protein. Here we present evidence that establishes the identity of F1-20 and AP-3. Monoclonal antibodies against F1-20 and AP-3 both specifically recognize a single protein from mouse brain with an apparent molecular mass of 190 kDa on SDS-PAGE. These monoclonal antibodies also specifically recognize the cloned F1-20 protein expressed in Escherichia coli. The anti-F1-20 monoclonal antibody (mAb) stains a bovine protein with an apparent molecular mass on SDS-PAGE of 190 kDa that copurifies with brain clathrin-coated vesicles (CCVs) and that can be extracted from the brain CCVs under conditions that extract AP-3. The anti-F1-20 and anti-AP-3 mAbs specifically recognize the same spot on a two-dimensional gel run on a bovine brain clathrin-coated vesicle extract. AP-3 purified from bovine brain CCVs is recognized by both the anti-F1-20 and anti-AP-3 mAbs. Purified preparations of bovine AP-3 and bacterially expressed mouse F1-20 give identical patterns of protease digestion with bromelain and subtilisin. Sequence analyses reveal that F1-20 has an essentially neutral 30-kDa NH2-terminal domain with an amino acid composition typical of a globular structure and an acidic COOH-terminal domain rich in proline, serine, threonine, and alanine. This is consistent with proteolysis experiments that suggested that AP-3 could be divided into a 30-kDa globular uncharged clathrin-binding domain and an acidic, anomalously migrating domain.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12655-62
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:7685348-Adaptor Proteins, Vesicular Transport, pubmed-meshheading:7685348-Alternative Splicing, pubmed-meshheading:7685348-Amino Acids, pubmed-meshheading:7685348-Animals, pubmed-meshheading:7685348-Antibodies, Monoclonal, pubmed-meshheading:7685348-Base Sequence, pubmed-meshheading:7685348-Blotting, Western, pubmed-meshheading:7685348-Brain Chemistry, pubmed-meshheading:7685348-Cattle, pubmed-meshheading:7685348-Cloning, Molecular, pubmed-meshheading:7685348-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:7685348-Gene Expression, pubmed-meshheading:7685348-Mice, pubmed-meshheading:7685348-Molecular Sequence Data, pubmed-meshheading:7685348-Molecular Weight, pubmed-meshheading:7685348-Monomeric Clathrin Assembly Proteins, pubmed-meshheading:7685348-Nerve Tissue Proteins, pubmed-meshheading:7685348-Oligodeoxyribonucleotides, pubmed-meshheading:7685348-Open Reading Frames, pubmed-meshheading:7685348-Phosphoproteins, pubmed-meshheading:7685348-Polymerase Chain Reaction, pubmed-meshheading:7685348-RNA
pubmed:year
1993
pubmed:articleTitle
The synapse-specific phosphoprotein F1-20 is identical to the clathrin assembly protein AP-3.
pubmed:affiliation
Department of Biological Sciences, University of Pittsburgh, Pennsylvania 15260.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't