Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 22
pubmed:dateCreated
2001-12-12
pubmed:abstractText
FENS-1 and DFCP1 are recently discovered proteins containing one or two FYVE-domains respectively. We show that the FYVE domains in these proteins can bind PtdIns3P in vitro with high specificity over other phosphoinositides. Exogenously expressed FENS-1 localises to early endosomes: this localisation requires an intact FYVE domain and is sensitive to wortmannin inhibition. The isolated FYVE domain of FENS-1 also localises to endosomes. These results are consistent with current models of FYVE-domain function in this cellular compartment. By contrast, exogenously expressed DFCP1 displays a predominantly Golgi, endoplasmic reticulum (ER) and vesicular distribution with little or no overlap with FENS-1 or other endosomal markers. Overexpression of DFCP1 was found to cause dispersal of the Golgi compartment defined by giantin and gpp130-staining. Disruption of the FYVE domains of DFCP1 causes a shift to more condensed and compact Golgi structures and overexpression of this mutant was found to confer significant protection to the Golgi against brefeldin-induced dispersal. These properties of DFCP1 are surprising, and suggest FYVE domain-localisation and function may not be exclusively endosomal. Movies available on-line
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Androstadienes, http://linkedlifedata.com/resource/pubmed/chemical/Brefeldin A, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Indicators and Reagents, http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Lipids, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol Phosphates, http://linkedlifedata.com/resource/pubmed/chemical/Protein Synthesis Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/ZFYVE1 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/macrogolgin, http://linkedlifedata.com/resource/pubmed/chemical/phosphatidylinositol 3-phosphate, http://linkedlifedata.com/resource/pubmed/chemical/wortmannin
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9533
pubmed:author
pubmed:issnType
Print
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3991-4000
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11739631-Androstadienes, pubmed-meshheading:11739631-Animals, pubmed-meshheading:11739631-Brefeldin A, pubmed-meshheading:11739631-COS Cells, pubmed-meshheading:11739631-Carrier Proteins, pubmed-meshheading:11739631-Endosomes, pubmed-meshheading:11739631-Enzyme Inhibitors, pubmed-meshheading:11739631-Golgi Apparatus, pubmed-meshheading:11739631-Green Fluorescent Proteins, pubmed-meshheading:11739631-Humans, pubmed-meshheading:11739631-Indicators and Reagents, pubmed-meshheading:11739631-Luminescent Proteins, pubmed-meshheading:11739631-Membrane Lipids, pubmed-meshheading:11739631-Membrane Proteins, pubmed-meshheading:11739631-Phosphatidylinositol Phosphates, pubmed-meshheading:11739631-Protein Binding, pubmed-meshheading:11739631-Protein Structure, Tertiary, pubmed-meshheading:11739631-Protein Synthesis Inhibitors, pubmed-meshheading:11739631-Protein Transport, pubmed-meshheading:11739631-Proteins, pubmed-meshheading:11739631-Recombinant Fusion Proteins, pubmed-meshheading:11739631-Surface Plasmon Resonance, pubmed-meshheading:11739631-Zinc Fingers
pubmed:year
2001
pubmed:articleTitle
FENS-1 and DFCP1 are FYVE domain-containing proteins with distinct functions in the endosomal and Golgi compartments.
pubmed:affiliation
Inositide Laboratory, The Babraham Institute, Babraham, Cambridge CB2 4AT, UK.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't