Linked Life Data

9193672

Source:http://linkedlifedata.com/resource/pubmed/id/9193672

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1997-9-4
pubmed:abstractText
Brefeldin A (BFA), a fungal metabolite that inhibits membrane transport, potently stimulates an endogenous ADP-ribosylation reaction that selectively modifies two cytosolic proteins of 38 and 50 kDa on an amino acid residue different from those used by all known mADPRTs. The 38-kDa substrate was identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH), whereas the 50-kDa substrate (BARS-50) was characterized as a novel guanine nucleotide binding protein. Thus, BARS-50 is able to bind GTP and its ADP-ribosylation is inhibited by the beta gamma subunit of GTP-binding (G) proteins. Moreover, BARS-50 was demonstrated to be a group of closely related proteins that appear to be different from all the known G proteins. A partially purified BARS-50 was obtained from rat brain cytosol, which was then used for microsequencing and in functional studies. A similar procedure led to the purification of native (non-ADP-ribosylated) BARS-50. The possible role of the BFA-dependent ADP-ribosylation and of BARS-50 in the maintenance of Golgi structure and function was addressed by examining which of the effects of BFA may be modified by inhibiting this reaction. We find that the BFA-dependent transformation of the Golgi stacks into a tubular reticular network is prevented when the BFA-dependent ADP-ribosylation activity was blocked by specific inhibitors thus indicating that BFA-dependent ADP-ribosylation of cytosolic proteins participate in the dynamic regulation of intracellular transport.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0065-2598
pubmed:author
pubmed:issnType
Print
pubmed:volume
419
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
321-30
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Possible role of BARS-50, a substrate of brefeldin A-dependent mono-ADP-ribosylation, in intracellular transport.
pubmed:affiliation
Department of Cell Biology and Oncology, Istituto di Ricerche Farmacologiche Mario Negri, Santa Maria Imbaro (Chieti), Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't