Linked Life Data

15358789

Source:http://linkedlifedata.com/resource/pubmed/id/15358789

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
47
pubmed:dateCreated
2004-11-15
pubmed:abstractText
The key gluconeogenic enzyme fructose-1,6-bisphosphatase (FBPase) is subjected to catabolite inactivation and degradation when glucose-starved cells are replenished with fresh glucose. In various studies, the proteasome and the vacuole have each been reported to be the major site of FBPase degradation. Because different growth conditions were used in these studies, we examined whether variations in growth conditions could alter the site of FBPase degradation. Here, we demonstrated that FBPase was degraded outside the vacuole (most likely in the proteasome), when glucose was added to cells that were grown in low glucose media for a short period of time. By contrast, cells that were grown in the same low glucose media for longer periods of time degraded FBPase in the vacuole in response to glucose. Another gluconeogenic enzyme malate dehydrogenase (MDH2) showed the same degradation characteristics as FBPase in that the short term starvation of cells led to a non-vacuolar degradation, whereas long term starvation resulted in the vacuolar degradation of this protein. The N-terminal proline is required for the degradation of FBPase and MDH2 for both the vacuolar and non-vacuolar proteolytic pathways. The cAMP signaling pathway and the phosphorylation of glucose were needed for the vacuolar-dependent degradation of FBPase and MDH2. By contrast, the cAMP-dependent signaling pathway was not involved in the non-vacuolar degradation of these proteins, although the phosphorylation of glucose was required.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
19
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49138-50
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:15358789-Binding Sites, pubmed-meshheading:15358789-Centrifugation, pubmed-meshheading:15358789-Cyclic AMP, pubmed-meshheading:15358789-DNA Primers, pubmed-meshheading:15358789-Fructose-Bisphosphatase, pubmed-meshheading:15358789-Glucose, pubmed-meshheading:15358789-Green Fluorescent Proteins, pubmed-meshheading:15358789-Malate Dehydrogenase, pubmed-meshheading:15358789-Mutagenesis, pubmed-meshheading:15358789-Mutation, pubmed-meshheading:15358789-Open Reading Frames, pubmed-meshheading:15358789-Phosphorylation, pubmed-meshheading:15358789-Plasmids, pubmed-meshheading:15358789-Polymerase Chain Reaction, pubmed-meshheading:15358789-Proline, pubmed-meshheading:15358789-Protein Structure, Tertiary, pubmed-meshheading:15358789-Saccharomyces cerevisiae, pubmed-meshheading:15358789-Signal Transduction, pubmed-meshheading:15358789-Time Factors, pubmed-meshheading:15358789-Vacuoles
pubmed:year
2004
pubmed:articleTitle
Degradation of the gluconeogenic enzymes fructose-1,6-bisphosphatase and malate dehydrogenase is mediated by distinct proteolytic pathways and signaling events.
pubmed:affiliation
Department of Cellular and Molecular Physiology, Penn State University College of Medicine, Hershey, Pennsylvania 17033, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.