Linked Life Data

9614134

Source:http://linkedlifedata.com/resource/pubmed/id/9614134

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
24
pubmed:dateCreated
1998-7-13
pubmed:abstractText
Heterotrimeric G proteins have been implicated in the regulation of intracellular protein transport, but their mechanism of action remains unclear. In vivo, secretion of chromogranin B, tagged with the green fluorescent protein, was inhibited by the addition of a general activator of trimeric G proteins (AlF4-) to stably transfected Vero cells and resulted in an accumulation of the tagged protein in the Golgi apparatus. In an in vitro assay that reconstitutes intra-Golgi protein transport, we find that a membrane-bound and AlF4--sensitive factor is involved in the fusion reaction. To determine whether this effect is mediated by a heterotrimeric G protein localized to COPI-coated transport vesicles, we determined the presence of G proteins on these vesicles and found that they were segregated relative to the donor membranes. Because G proteins do not have an obvious sorting, retention, or retrieval signal, we considered the possibility that other interactions might be responsible for this segregation. In agreement with this, we found that trimeric G proteins from isolated Golgi membranes were partially insoluble in Triton X-100. Identification of the proteins that interact with the heterotrimeric G proteins in the Golgi-derived detergent-insoluble complex might help to reveal the regulation of protein secretion mediated by heterotrimeric G proteins.
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
12
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
15203-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9614134-Aluminum Compounds, pubmed-meshheading:9614134-Animals, pubmed-meshheading:9614134-Cell Line, pubmed-meshheading:9614134-Chromogranins, pubmed-meshheading:9614134-Coated Vesicles, pubmed-meshheading:9614134-Coatomer Protein, pubmed-meshheading:9614134-Detergents, pubmed-meshheading:9614134-Fluorides, pubmed-meshheading:9614134-GTP-Binding Proteins, pubmed-meshheading:9614134-Golgi Apparatus, pubmed-meshheading:9614134-Green Fluorescent Proteins, pubmed-meshheading:9614134-Guanosine Triphosphate, pubmed-meshheading:9614134-Luminescent Proteins, pubmed-meshheading:9614134-Membrane Fusion, pubmed-meshheading:9614134-Membrane Proteins, pubmed-meshheading:9614134-Microscopy, Fluorescence, pubmed-meshheading:9614134-Protein Conformation, pubmed-meshheading:9614134-Solubility, pubmed-meshheading:9614134-Transfection
pubmed:year
1998
pubmed:articleTitle
A putative heterotrimeric G protein inhibits the fusion of COPI-coated vesicles. Segregation of heterotrimeric G proteins from COPI-coated vesicles.
pubmed:affiliation
Biochemie-Zentrum Heidelberg (BZH), University of Heidelberg, Im Neuenheimer Feld 328, 69120 Heidelberg, Germany. Helms@urz.uni-heidelberg.de
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't