Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1997-5-1
pubmed:abstractText
The multi-functional protein calreticulin (CRT) is normally found within the lumen of the endoplasmic reticulum (ER). However, some of its proposed functions require it to be located within the nucleus, where its presence is contentious. We have investigated this in live COS7, HeLa and LM(TK-) cells using green fluorescent protein (GFP)-fusion proteins. GFP-CRT, and GFP, with an ER signal peptide and a KDEL sequence (ER-GFP), were localised to the ER. In addition, GFP-CRT was located in the nucleus of all the cell types at low levels. The higher levels of nuclear fluorescence in LM(TK-) and HeLa cells suggested that glucocorticoid receptors might enhance nuclear localisation of calreticulin. Dexamethasone treatment of LM(TK-) cells doubled the amount of nuclear GFP-CRT, but did not affect the localisation of a GFP-CRT fusion in which the glucocorticoid receptor-binding N-domain of calreticulin had been deleted. Thus, despite ER targeting and retention signals, calreticulin is also located within the nucleus where its presence increases due to its interaction with glucocorticoid receptors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Calreticulin, http://linkedlifedata.com/resource/pubmed/chemical/Dexamethasone, http://linkedlifedata.com/resource/pubmed/chemical/Glucocorticoids, http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Oligopeptides, http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Glucocorticoid, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, http://linkedlifedata.com/resource/pubmed/chemical/lysyl-aspartyl-glutamyl-leucine
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
405
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
181-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9089287-Animals, pubmed-meshheading:9089287-COS Cells, pubmed-meshheading:9089287-Calcium-Binding Proteins, pubmed-meshheading:9089287-Calreticulin, pubmed-meshheading:9089287-Cell Compartmentation, pubmed-meshheading:9089287-Cell Nucleus, pubmed-meshheading:9089287-Dexamethasone, pubmed-meshheading:9089287-Endoplasmic Reticulum, pubmed-meshheading:9089287-Glucocorticoids, pubmed-meshheading:9089287-Green Fluorescent Proteins, pubmed-meshheading:9089287-HeLa Cells, pubmed-meshheading:9089287-Humans, pubmed-meshheading:9089287-Immunohistochemistry, pubmed-meshheading:9089287-Luminescent Proteins, pubmed-meshheading:9089287-Oligopeptides, pubmed-meshheading:9089287-Protein Sorting Signals, pubmed-meshheading:9089287-Receptors, Glucocorticoid, pubmed-meshheading:9089287-Recombinant Fusion Proteins, pubmed-meshheading:9089287-Ribonucleoproteins
pubmed:year
1997
pubmed:articleTitle
Nuclear localisation of calreticulin in vivo is enhanced by its interaction with glucocorticoid receptors.
pubmed:affiliation
Department of Medical Biochemistry, University of Wales College of Medicine, Cardiff, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't