Linked Life Data

9446595

Source:http://linkedlifedata.com/resource/pubmed/id/9446595

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1998-2-23
pubmed:databankReference
pubmed:abstractText
Synaptogyrin is an abundant membrane protein of synaptic vesicles containing four transmembrane regions and a C-terminal cytoplasmic tail that is tyrosine phosphorylated. We have now identified a novel isoform of synaptogyrin called cellugyrin that exhibits 47% sequence identity with synaptogyrin. In rat tissues, cellugyrin and synaptogyrins are expressed in mirror image patterns. Cellugyrin is ubiquitously present in all tissues tested with the lowest levels in brain tissue, whereas synaptogyrin protein is only detectable in brain. Transfection studies in COS cells demonstrated that both cellugyrin and synaptogyrin are tyrosine phosphorylated in vivo by pp60c-src, and experiments with recombinant proteins showed that pp60c-src phosphorylates the cytoplasmic tails of these proteins in vitro. Cellugyrin and synaptogyrin co-localize when transfected into COS cells but are differentially distributed in brain, the only tissue where both proteins are detectable. Our data suggest that the synaptic vesicle protein synaptogyrin is a specialized version of a ubiquitous protein, cellugyrin, with the two proteins sharing structural similarity but differing in localization. This finding supports the emerging concept of synaptic vesicles as the simplified and specialized form of a generic trafficking organelle. The conserved tyrosine phosphorylation of cellugyrin and synaptogyrins suggests a link between tyrosine phosphorylation via pp60c-src and membrane traffic.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2851-7
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9446595-Amino Acid Sequence, pubmed-meshheading:9446595-Animals, pubmed-meshheading:9446595-Biological Transport, pubmed-meshheading:9446595-Cell Compartmentation, pubmed-meshheading:9446595-Cloning, Molecular, pubmed-meshheading:9446595-Exocytosis, pubmed-meshheading:9446595-Membrane Glycoproteins, pubmed-meshheading:9446595-Membrane Proteins, pubmed-meshheading:9446595-Molecular Sequence Data, pubmed-meshheading:9446595-Nerve Tissue Proteins, pubmed-meshheading:9446595-Phosphorylation, pubmed-meshheading:9446595-Proto-Oncogene Proteins pp60(c-src), pubmed-meshheading:9446595-Rats, pubmed-meshheading:9446595-Sequence Analysis, DNA, pubmed-meshheading:9446595-Sequence Homology, Amino Acid, pubmed-meshheading:9446595-Synaptophysin, pubmed-meshheading:9446595-Tissue Distribution
pubmed:year
1998
pubmed:articleTitle
Cellugyrin, a novel ubiquitous form of synaptogyrin that is phosphorylated by pp60c-src.
pubmed:affiliation
Department of Molecular Genetics and Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, Dallas, Texas 75235, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't