rdf:type |
|
lifeskim:mentions |
umls-concept:C0031603,
umls-concept:C0031621,
umls-concept:C0037083,
umls-concept:C0127400,
umls-concept:C0205369,
umls-concept:C1167622,
umls-concept:C1260969,
umls-concept:C1514562,
umls-concept:C1710082,
umls-concept:C1880389,
umls-concept:C1882954,
umls-concept:C1883204,
umls-concept:C1883221
|
pubmed:issue |
1
|
pubmed:dateCreated |
1998-8-31
|
pubmed:abstractText |
Phosphoinositide 3-kinases (PI(3)K) are important regulators of receptor signaling cascades and intracellular membrane trafficking. To date, no protein domain has been identified that binds specifically to Ptdlns(3)P and thereby recruits/activates downstream effectors of Ptdlns(3)P signaling. Using an in vivo assay in yeast that detects Vps34 PI(3)K-dependent intracellular localization of a GFP reporter protein, and in vitro lipid-binding assays, we demonstrate that cysteine-rich RING domains of the FYVE finger subfamily bind specifically to Ptdlns phosphorylated exclusively at the D-3 position of the inositol ring. GFP-FYVE domain fusion proteins localized predominantly to membranes of endocytic compartments and required active Vps34 PI(3)K. Our data establish a molecular link between Vps34 PI(3)K and several FYVE domain-containing proteins (Vac1p, Vps27p) required for vacuolar/lysosomal protein trafficking.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
1097-2765
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
2
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
157-62
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:9702203-Binding Sites,
pubmed-meshheading:9702203-Biological Transport,
pubmed-meshheading:9702203-Cell Compartmentation,
pubmed-meshheading:9702203-Fungal Proteins,
pubmed-meshheading:9702203-Genes, Reporter,
pubmed-meshheading:9702203-Green Fluorescent Proteins,
pubmed-meshheading:9702203-Liposomes,
pubmed-meshheading:9702203-Luminescent Proteins,
pubmed-meshheading:9702203-Lysosomes,
pubmed-meshheading:9702203-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:9702203-Phosphatidylinositol Phosphates,
pubmed-meshheading:9702203-Phosphorylation,
pubmed-meshheading:9702203-Protein Binding,
pubmed-meshheading:9702203-Recombinant Fusion Proteins,
pubmed-meshheading:9702203-Saccharomyces cerevisiae,
pubmed-meshheading:9702203-Signal Transduction,
pubmed-meshheading:9702203-Vacuoles,
pubmed-meshheading:9702203-Zinc Fingers
|
pubmed:year |
1998
|
pubmed:articleTitle |
Phosphatidylinositol(3)-phosphate signaling mediated by specific binding to RING FYVE domains.
|
pubmed:affiliation |
Howard Hughes Medical Institute, University of California, San Diego School of Medicine, La Jolla 92093-0668, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|