Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2011-6-9
pubmed:abstractText
In a variety of organisms, including worms, flies, and mammals, glucose homeostasis is maintained by insulin-like signaling in a robust network of opposing and complementary signaling pathways. The hexosamine signaling pathway, terminating in O-linked-N-acetylglucosamine (O-GlcNAc) cycling, is a key sensor of nutrient status and has been genetically linked to the regulation of insulin signaling in Caenorhabditis elegans. Here we demonstrate that O-GlcNAc cycling and insulin signaling are both essential components of the C. elegans response to glucose stress. A number of insulin-dependent processes were found to be sensitive to glucose stress, including fertility, reproductive timing, and dauer formation, yet each of these differed in their threshold of sensitivity to glucose excess. Our findings suggest that O-GlcNAc cycling and insulin signaling are both required for a robust and adaptable response to glucose stress, but these two pathways show complex and interdependent roles in the maintenance of glucose-insulin homeostasis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine, http://linkedlifedata.com/resource/pubmed/chemical/Caenorhabditis elegans Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Carbohydrates, http://linkedlifedata.com/resource/pubmed/chemical/DAF-2 protein, C elegans, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/Insulin, http://linkedlifedata.com/resource/pubmed/chemical/Lipids, http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylglucosaminyltransferases, http://linkedlifedata.com/resource/pubmed/chemical/O-GlcNAc transferase, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin, http://linkedlifedata.com/resource/pubmed/chemical/beta-N-Acetylhexosaminidases, http://linkedlifedata.com/resource/pubmed/chemical/hexosaminidase C
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1943-2631
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
188
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
369-82
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:21441213-Acetylglucosamine, pubmed-meshheading:21441213-Animals, pubmed-meshheading:21441213-Blotting, Western, pubmed-meshheading:21441213-Caenorhabditis elegans, pubmed-meshheading:21441213-Caenorhabditis elegans Proteins, pubmed-meshheading:21441213-Carbohydrates, pubmed-meshheading:21441213-Dose-Response Relationship, Drug, pubmed-meshheading:21441213-Female, pubmed-meshheading:21441213-Glucose, pubmed-meshheading:21441213-Insulin, pubmed-meshheading:21441213-Larva, pubmed-meshheading:21441213-Lipids, pubmed-meshheading:21441213-Male, pubmed-meshheading:21441213-Mutation, pubmed-meshheading:21441213-N-Acetylglucosaminyltransferases, pubmed-meshheading:21441213-Receptor, Insulin, pubmed-meshheading:21441213-Reproduction, pubmed-meshheading:21441213-Signal Transduction, pubmed-meshheading:21441213-Stress, Physiological, pubmed-meshheading:21441213-Time Factors, pubmed-meshheading:21441213-beta-N-Acetylhexosaminidases
pubmed:year
2011
pubmed:articleTitle
O-linked-N-acetylglucosamine cycling and insulin signaling are required for the glucose stress response in Caenorhabditis elegans.
pubmed:affiliation
Department of Biology, College of the Holy Cross, Worcester, Massachusetts 01610, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Intramural