Linked Life Data

10383386

Source:http://linkedlifedata.com/resource/pubmed/id/10383386

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1999-7-27
pubmed:databankReference
pubmed:abstractText
Synaptogyrins constitute a family of synaptic vesicle proteins of unknown function. With the full-length structure of a new brain synaptogyrin isoform, we now show that the synaptogyrin family in vertebrates includes two neuronal and one ubiquitous isoform. All of these synaptogyrins are composed of a short conserved N-terminal cytoplasmic sequence, four homologous transmembrane regions, and a variable cytoplasmic C-terminal tail that is tyrosine-phosphorylated. The localization, abundance, and conservation of synaptogyrins suggest a function in exocytosis. To test this, we employed a secretion assay in PC12 cells expressing transfected human growth hormone (hGH) as a reporter protein. When Ca2+-dependent hGH secretion from PC12 cells was triggered by high K+ or alpha-latrotoxin, co-transfection of all synaptogyrins with hGH inhibited hGH exocytosis as strongly as co-transfection of tetanus toxin light chain. Synaptophysin I, which is distantly related to synaptogyrins, was also inhibitory but less active. Inhibition was independent of the amount of hGH expressed but correlated with the amount of synaptogyrin transfected. Inhibition of exocytosis was not observed with several other synaptic proteins, suggesting specificity. Analysis of the regions of synaptogyrin required for inhibition revealed that the conserved N-terminal domain of synaptogyrin is essential for inhibition, whereas the long C-terminal cytoplasmic tail is largely dispensable. Our results suggest that synaptogyrins are conserved components of the exocytotic apparatus, which function as regulators of Ca2+-dependent exocytosis.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
274
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
18893-901
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:10383386-Amino Acid Sequence, pubmed-meshheading:10383386-Animals, pubmed-meshheading:10383386-COS Cells, pubmed-meshheading:10383386-Calcium, pubmed-meshheading:10383386-Conserved Sequence, pubmed-meshheading:10383386-Exocytosis, pubmed-meshheading:10383386-Human Growth Hormone, pubmed-meshheading:10383386-Humans, pubmed-meshheading:10383386-Membrane Proteins, pubmed-meshheading:10383386-Mice, pubmed-meshheading:10383386-Mice, Knockout, pubmed-meshheading:10383386-Molecular Sequence Data, pubmed-meshheading:10383386-Nerve Tissue Proteins, pubmed-meshheading:10383386-PC12 Cells, pubmed-meshheading:10383386-Potassium, pubmed-meshheading:10383386-Rats, pubmed-meshheading:10383386-Sequence Homology, Amino Acid, pubmed-meshheading:10383386-Spider Venoms, pubmed-meshheading:10383386-Synaptophysin, pubmed-meshheading:10383386-Tetanus Toxin
pubmed:year
1999
pubmed:articleTitle
Synaptogyrins regulate Ca2+-dependent exocytosis in PC12 cells.
pubmed:affiliation
Center for Basic Neuroscience, Department of Molecular Genetics and Howard Hughes Medical Institute, The University of Texas Southwestern Medical Center, Dallas, Texas 75235-9050, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't